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	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4169</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4169"/>
		<updated>2010-03-01T10:47:25Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998 Ducros2003&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[general acid/base]] has been inferred by homology to GH16, the other family in clan GH-B, where it has been verified by azide rescue of inactivated mutants of a ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bend around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of ''Hypocrea jecorina'' Cel7A revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a covalent 2-deoxy-2-fluorocellotriosyl enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Suggested by structural studies and mutation in ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994 Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;. Verified in ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase of GH16 by azide rescue of inactivated mutants &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I; Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Ducros2003 pmid=12890535&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Viladot1998 pmid=9698381&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4168</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4168"/>
		<updated>2010-03-01T10:42:32Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998 Ducros2003&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[general acid/base]] has been inferred by homology to GH16, the other family in clan GH-B, where it has been verified by azide rescue of inactivated mutants of a ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bend around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of ''Hypocrea jecorina'' Cel7A revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a covalent 2-deoxy-2-fluorocellotriosyl enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Suggested by structural studies and mutation in ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994 Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;. Verified in ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase of GH16 by azide rescue of inactivated mutants &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Ducros2003 pmid=12890535&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Viladot1998 pmid=9698381&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4167</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4167"/>
		<updated>2010-03-01T10:40:24Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998 Ducros2003&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[general acid/base]] has been inferred by homology to GH16, the other family in clan GH-B, where it has been verified by azide rescue of inactivated mutants of a ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bends around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of ''Hypocrea jecorina'' Cel7A revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a covalent 2-deoxy-2-fluorocellotriosyl enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Suggested by structural studies and mutation in ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994 Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;. Verified in ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase of GH16 by azide rescue of inactivated mutants &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Ducros2003 pmid=12890535&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Viladot1998 pmid=9698381&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4166</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4166"/>
		<updated>2010-03-01T10:15:04Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[general acid/base]] has been inferred by homology to GH16, the other family in clan GH-B, where it has been verified by azide rescue of inactivated mutants of a ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bends around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of ''Hypocrea jecorina'' Cel7A revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a covalent 2-deoxy-2-fluorocellotriosyl enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Suggested by structural studies and mutation in ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994 Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;. Verified in ''Bacillus licheniformis'' 1,3-1,4-&amp;amp;beta;-D-glucan 4-glucanohydrolase of GH16 by azide rescue of inactivated mutants &amp;lt;cite&amp;gt;Viladot1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Viladot1998 pmid=9698381&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4165</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4165"/>
		<updated>2010-03-01T09:47:34Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bends around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of ''Hypocrea jecorina'' Cel7A revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4164</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4164"/>
		<updated>2010-03-01T09:43:17Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bends around the active site so that a more or less closed tunnel is formed through the enzyme. Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of Hypocrea jecorina Cel7A &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;, revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4163</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4163"/>
		<updated>2010-03-01T09:41:25Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Three-dimensional structures are available for both endoglucanases and cellobiohydrolases of GH7. The first cellobiohydrolase structure, the catalytic module of ''Hypocrea jecorina'' Cel7A, was published in 1994 (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, and the first endoglucanase, ''Fusarium oxysporum'' EG I (Cel7B), in 1996 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;. The proteins are built up around a &amp;amp;beta;-jellyroll folded framework, in which two large anti-parallell &amp;amp;beta;-sheets pack face-to-face to form a highly curved &amp;amp;beta;-sandwich. The &amp;amp;beta;-sandwich is further extended along both edges by several of the loops that connect the &amp;amp;beta;-strands, resulting in a long (~50 &amp;amp;Aring;) substrate-binding surface that runs perpendicular to the &amp;amp;beta;-strands of the inner, concave &amp;amp;beta;-sheet. A few short &amp;amp;alpha;-helical segments occur in some of the loops at the perifery of the structure. Endoglucanases have an open substrate binding cleft/groove, while in cellobiohydrolases some loops are further elongated and bends around the active site so that a more or less closed tunnel is formed through the enzyme. &lt;br /&gt;
&lt;br /&gt;
Further structural studies have provided detailed knowledge about catalytic mechanism and substrate binding in family 7. Some key studies include: &lt;br /&gt;
&lt;br /&gt;
i) A complex of ''Fusarium oxysporum'' EG1 (Cel7B) with a non-hydrolysable substrate analog (thio-cellopentaose) indicated that transition of the glucose residue at site -1 from a &amp;lt;sup&amp;gt;4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;C&amp;lt;/i&amp;gt;&amp;lt;sub&amp;gt;1&amp;lt;/sub&amp;gt; chair to a distorted &amp;lt;sup&amp;gt;1,4&amp;lt;/sup&amp;gt;&amp;lt;i&amp;gt;B&amp;lt;/i&amp;gt; boat conformation is reqiured prior to hydrolysis ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
ii) Cellooligosaccharides bound in catalytically deficient mutants of Hypocrea jecorina Cel7A &amp;lt;cite&amp;gt;Stahlberg1996 Divne1998&amp;lt;/cite&amp;gt;, revealed 10 discrete glucosyl-binding subsites, -7 to +3, and allowed modelling of a productively bound cellulose chain along the entire tunnel of the enzyme.&lt;br /&gt;
&lt;br /&gt;
iii) The discovery of two discrete binding modes for cellobiose in the product sites +1/+2 in ''Hypocrea jecorina'' Cel7A and ''Phanerochaete chrysosporium'' Cel7D, indicated that hydrolysis of the glycosyl-enzyme intermediate may proceed without prior release of the cellobiose product, and suggests a product ejection mechanism during processive hydrolysis of cellulose &amp;lt;cite&amp;gt;Ubhayasekera2005&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
iv) Later studies of oligosaccharide binding in ''Melanocarpus albomyces'' Cel7B provide further insight into the flexibility of sugar binding within the tunnel of a cellobiohydrolase &amp;lt;cite&amp;gt;Parkkinen2008&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#Divne1998 pmid=9466911&lt;br /&gt;
&lt;br /&gt;
#Ubhayasekera2005 pmid=15819888&lt;br /&gt;
&lt;br /&gt;
#Parkkinen2008 pmid=18499583&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4150</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4150"/>
		<updated>2010-02-25T16:51:04Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''Hypocrea jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''Hypocrea jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''Humicola insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''Hypocrea jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''Fusarium oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''Humicola insolens'' Cel7B by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4149</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4149"/>
		<updated>2010-02-25T16:48:08Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''H. jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''H. jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''H. insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Suggested in ''H. jecorina'' cellobiohydrolase Cel7A &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt; and ''F. oxysporum'' endoglucanase Cel7B &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt; via affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside. Verified in ''H. insolens'' Cel7B by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4145</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4145"/>
		<updated>2010-02-25T16:09:07Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''H. jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''H. jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate in ''H. insolens'' Cel7B and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4144</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4144"/>
		<updated>2010-02-25T16:06:00Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
In GH7 enzymes the catalytic residues are positioned close to each other in sequence in the consensus motif -Glu-X-Asp-X-X-Glu-, where the first Glu acts as [[catalytic nucleophile]] and the other Glu as [[general acid/base]]. This was proposed in the first 3-D structure publication, of ''H. jecorina'' Cel7A &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;, based on the position of the residues relative to a ''o''-iodo-benzyl-cellobioside molecule bound at the active site. It was supported by mutational studies with the same enzyme &amp;lt;cite&amp;gt;Stahlberg1996&amp;lt;/cite&amp;gt;, which also showed that the Aspartate residue in the consensus motif is important for catalysis, and with Endoglucanase I (EG I, Cel7B) from ''Humicola insolens'' &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. The [[catalytic nucleophile]] was further supported by affinity labelling with 3,4-epoxybutyl-&amp;amp;beta;-cellobioside; with ''H. jecorina'' Cel7A the identification was done by ESI-MS peptide mapping and sequencing &amp;lt;cite&amp;gt;Klarskov1997&amp;lt;/cite&amp;gt;, and with ''Fusarium oxysporum'' Endoglucanase I (EG I, Cel7B) the residue was identified by X-ray crystallography &amp;lt;cite&amp;gt;Sulzenbacher1997&amp;lt;/cite&amp;gt;. This was subsequently verified by trapping of a 2-deoxy-2-fluorocellotriosyl covalent enzyme intermediate and identification of the labelled peptide by tandem MS &amp;lt;cite&amp;gt;Mackenzie1998&amp;lt;/cite&amp;gt;. &lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Stahlberg1996 pmid=8951380&lt;br /&gt;
&lt;br /&gt;
#Mackenzie1998 pmid=9761741&lt;br /&gt;
&lt;br /&gt;
#Klarskov1997 pmid=9449766&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1997 pmid=9153432&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4140</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4140"/>
		<updated>2010-02-24T22:40:06Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'' &amp;lt;cite&amp;gt;Kuhls1996&amp;lt;/cite&amp;gt;).&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Kuhls1996 pmid=8755548&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4139</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4139"/>
		<updated>2010-02-24T22:06:25Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'').&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4138</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4138"/>
		<updated>2010-02-24T22:03:22Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'').&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1OVW PDB 1ovw]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Jonathan K. C. Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4137</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4137"/>
		<updated>2010-02-24T22:01:46Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I (CBH I; Cel7A) from the fungus ''Trichoderma reesei'' (a clonal derivative of ''Hypocrea jecorina'').&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1BYH PDB 1byh]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Jonathan K. C. Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4136</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4136"/>
		<updated>2010-02-24T21:53:29Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I, CBH I, later called Cel7A, from the fungus ''Trichoderma reesei'', which has later been identified as a clonal derivative of ''Hypocrea jecorina''.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1BYH PDB 1byh]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Jonathan K. C. Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4135</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=4135"/>
		<updated>2010-02-24T21:50:59Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Most [[Glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose/&amp;amp;beta;-1,4-glucans. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4), [reducing end-acting] cellobiohydrolase (EC 3.2.1.-), chitosanase (EC 3.2.1.132) and ''[[endo]]''-1,3-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.73).&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Family 7 enzymes are [[retaining]] enzymes, as first shown by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt; on Cellobiohydrolase I, CBH I, later called Cel7A, from the fungus ''Trichoderma reesei'', which has later been identified as a clonal derivative of ''Hypocrea jecorina''.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: ''Hypocrea jecorina'' cellobiohydrolase Cel7A by NMR &amp;lt;cite&amp;gt;Knowles1988&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: First cellobiohydrolase was ''Hypocrea jecorina'' Cel7A (CBH I; [http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEL PDB 1cel]) &amp;lt;cite&amp;gt;Divne1994&amp;lt;/cite&amp;gt;. First ''[[endo]]''-1,4-&amp;amp;beta;-glucanase was Endoglucanase I (EG I, Cel7B) from ''Fusarium oxysporum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1BYH PDB 1byh]) &amp;lt;cite&amp;gt;Sulzenbacher1996&amp;lt;/cite&amp;gt;, both by X-ray crystallography.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Knowles1988 Jonathan K. C. Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of ''Trichoderma reesei''. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. [http://dx.doi.org/10.1039/C39880001401 DOI: 10.1039/C39880001401]&lt;br /&gt;
&lt;br /&gt;
#Divne1994 pmid=8036495&lt;br /&gt;
&lt;br /&gt;
#Sulzenbacher1996 pmid=8952478&lt;br /&gt;
&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Glycoside Hydrolase Families|GH007]]&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=3059</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=3059"/>
		<updated>2009-12-30T15:39:27Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please delete the {{UnderConstruction}} tag below when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
[[Glycoside hydrolases]] of family 7 cleave &amp;amp;beta;-1,4 glycosidic bonds in cellulose. Several members also show activity on xylan. The substrate specificities found in GH7 are: ''[[endo]]''-1,4-&amp;amp;beta;-glucanase (EC 3.2.1.4); [reducing end-acting] cellobiohydrolase (EC 3.2.1.-) and chitosanase (EC 3.2.1.132).&lt;br /&gt;
&lt;br /&gt;
This is an example of how to make references to a journal article &amp;lt;cite&amp;gt;Comfort2007&amp;lt;/cite&amp;gt;. (See the References section below).  Multiple references can go in the same place like this &amp;lt;cite&amp;gt;Comfort2007 He1999&amp;lt;/cite&amp;gt;.  You can even cite books using just the ISBN &amp;lt;cite&amp;gt;3&amp;lt;/cite&amp;gt;.  References that are not in PubMed can be typed in by hand &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.  &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;Comfort2007&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;3&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Comfort2007 pmid=17323919&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- ATTN CURATOR: Please delete the &amp;quot;&amp;lt;nowiki&amp;gt;&amp;quot; and &amp;quot;&amp;lt;/nowiki&amp;gt;&amp;quot; tags below when you are ready for the page to be included in the &amp;quot;GH Families&amp;quot; category, which is linked on the Main Page; ALSO: REPLACE &amp;quot;nnn&amp;quot; with the family number) --&amp;gt;&lt;br /&gt;
&amp;lt;nowiki&amp;gt;[[Category:Glycoside Hydrolase Families|GHnnn]]&amp;lt;/nowiki&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=3058</id>
		<title>Glycoside Hydrolase Family 7</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_7&amp;diff=3058"/>
		<updated>2009-12-30T15:24:25Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- CURATORS: Please delete the {{UnderConstruction}} tag below when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]: ^^^Jerry Stahlberg^^^&lt;br /&gt;
* [[Responsible Curator]]:  ^^^Jerry Stahlberg^^^&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Glycoside Hydrolase Family 7'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Clan'''    &lt;br /&gt;
|GH-B&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|retaining&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |http://www.cazy.org/fam/GH7.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
This is an example of how to make references to a journal article &amp;lt;cite&amp;gt;Comfort2007&amp;lt;/cite&amp;gt;. (See the References section below).  Multiple references can go in the same place like this &amp;lt;cite&amp;gt;Comfort2007 He1999&amp;lt;/cite&amp;gt;.  You can even cite books using just the ISBN &amp;lt;cite&amp;gt;3&amp;lt;/cite&amp;gt;.  References that are not in PubMed can be typed in by hand &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.  &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;Comfort2007&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;MikesClassic&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;He1999&amp;lt;/cite&amp;gt;.&lt;br /&gt;
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation &amp;lt;cite&amp;gt;3&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Comfort2007 pmid=17323919&lt;br /&gt;
#He1999 pmid=9312086&lt;br /&gt;
#3 isbn=978-0-240-52118-3&lt;br /&gt;
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- ATTN CURATOR: Please delete the &amp;quot;&amp;lt;nowiki&amp;gt;&amp;quot; and &amp;quot;&amp;lt;/nowiki&amp;gt;&amp;quot; tags below when you are ready for the page to be included in the &amp;quot;GH Families&amp;quot; category, which is linked on the Main Page; ALSO: REPLACE &amp;quot;nnn&amp;quot; with the family number) --&amp;gt;&lt;br /&gt;
&amp;lt;nowiki&amp;gt;[[Category:Glycoside Hydrolase Families|GHnnn]]&amp;lt;/nowiki&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3057</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3057"/>
		<updated>2009-12-30T14:44:53Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Jerry_Stahlberg.jpg|right]]'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of ''Trichoderma'' cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of ''T. reesei'' CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3056</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3056"/>
		<updated>2009-12-30T14:41:23Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Jerry_Stahlberg.jpg|thumb|widthpx| ]]'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of ''Trichoderma'' cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of ''T. reesei'' CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3055</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3055"/>
		<updated>2009-12-30T14:40:08Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Jerry_Stahlberg.jpg]]'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of ''Trichoderma'' cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of ''T. reesei'' CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3054</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3054"/>
		<updated>2009-12-30T14:37:35Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Jerry_Stahlberg.jpg|thumb|widthpx| ]]'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of ''Trichoderma'' cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of ''T. reesei'' CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=File:Jerry_Stahlberg.jpg&amp;diff=3053</id>
		<title>File:Jerry Stahlberg.jpg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=File:Jerry_Stahlberg.jpg&amp;diff=3053"/>
		<updated>2009-12-30T14:31:03Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: uploaded a new version of &amp;quot;File:Jerry Stahlberg.jpg&amp;quot;:&amp;amp;#32;Jerry Stahlberg headshot&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Jerry Stahlberg headshot&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=File:Jerry_Stahlberg.jpg&amp;diff=3052</id>
		<title>File:Jerry Stahlberg.jpg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=File:Jerry_Stahlberg.jpg&amp;diff=3052"/>
		<updated>2009-12-30T14:28:46Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: Jerry Stahlberg headshot&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Jerry Stahlberg headshot&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3051</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3051"/>
		<updated>2009-12-30T13:27:12Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of ''Trichoderma'' cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of ''T. reesei'' CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3050</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3050"/>
		<updated>2009-12-30T13:26:15Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of Trichoderma cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of T. reesei CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3049</id>
		<title>User talk:Jerry Stahlberg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User_talk:Jerry_Stahlberg&amp;diff=3049"/>
		<updated>2009-12-30T13:24:01Z</updated>

		<summary type="html">&lt;p&gt;Jerry Stahlberg: Created page with '  '''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden. …'&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&lt;br /&gt;
&lt;br /&gt;
'''Jerry Ståhlberg''''s user page. I am an Associate Professor at Department of Molecular Biology at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden. Together with Dr. Mats Sandgren I am leading a research group where we study structure and function of carbohydrate-active enzymes, with particular interest in plant biomass degrading enzymes for various biofuel and biorefinery applications.&lt;br /&gt;
&lt;br /&gt;
Address: Jerry Stahlberg, Dept Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, PO Box 590, SE-751 24 Uppsala, Sweden. Phone: +46-(0)18-4714590. E-mail: jerry.stahlberg@molbio.slu.se&lt;br /&gt;
&lt;br /&gt;
I am a biochemist by education. My interest in CAZYmes started in the end of the 80's when I did my PhD with Dr. Göran Pettersson at Uppsala University, studying enzymology of Trichoderma cellulases. Through collaboration with Prof. Alwyn Jones in Uppsala, we were lucky to see the first 3D structures of cellulases, the NMR structure of a fungal CBM1 and the x-ray structure of the catalytic domain of T. reesei CBH2 (GH6). In 1993 I joined Alwyn Jones' group at Dept. Molecular Biology, Uppsala University, and worked with Christina Divne and others on structure/function studies of CAZymes, mainly fungal cellobiohydrolases of GH6 and GH7. In 1998 I was promoted to Associate Professor (Docent) in Moleular Biology at Uppsala University, and moved the same year to the Swedish University of Agricultural Sciences where I have a permanent position. Since 2009 I also hold a part-time professor-ship at the Norwegian University of Life Sciences (UMB), Ås, Norway.&lt;/div&gt;</summary>
		<author><name>Jerry Stahlberg</name></author>
	</entry>
</feed>