Glycoside Hydrolase Family 75 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:16:30Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: Updated to Curator Approved status on behalf of R. Brzezinski, ref. email dated 2011-06-07

2011-06-22T14:37:50Z

Updated to Curator Approved status on behalf of R. Brzezinski, ref. email dated 2011-06-07

Harry Brumer: fixed paragraph spacing

2011-06-22T14:36:50Z

fixed paragraph spacing

Ryszard Brzezinski at 20:36, 3 June 2011

2011-06-03T20:36:54Z

Ryszard Brzezinski at 20:17, 3 June 2011

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Ryszard Brzezinski at 20:15, 3 June 2011

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Ryszard Brzezinski at 19:56, 3 June 2011

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Ryszard Brzezinski at 19:53, 3 June 2011

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-* [[Author]]: ^^^Ryszard Brzezinski^^^
+* [[Author]]: [[User:Ryszard Brzezinski|Ryszard Brzezinski]]
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+* [[Responsible Curator]]:  [[User:Ryszard Brzezinski|Ryszard Brzezinski]]
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-<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
+{{CuratorApproved}}
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 * [[Responsible Curator]]:  ^^^Ryszard Brzezinski^^^

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 == Kinetics and Mechanism ==
 Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate  <cite>Cheng2006</cite>.
 == Catalytic Residues ==
 A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members.
 == Three-dimensional structures ==
 No three-dimensional structure has been solved for this family.
 == Family Firsts ==

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 == Substrate specificities ==
-Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.
+Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.
 == Kinetics and Mechanism ==

← Older revision		Revision as of 20:17, 3 June 2011
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	== Catalytic Residues ==		== Catalytic Residues ==
−	A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members	+	A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members.

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 == Catalytic Residues ==
-A site-directed mutagenesis study performed on the enzyme from ''Aspergillus fumigatus'' expressed as a recombinant protein in ''Escherichia coli'' showed that Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members
+A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members
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 #Cheng2006 pmid=16330537
 #Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.
 </biblio>

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 |-
 |'''Mechanism'''
-|inverting
+|Inverting
 |-
 |'''Active site residues'''
-|known
+|Inferred
 |-
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
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 == Kinetics and Mechanism ==
-Family GH46 enzymes utilize an inverting mechanism as shown by NMR <cite>Cheng2006</cite>.
+Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate  <cite>Cheng2006</cite>.
 == Catalytic Residues ==
-Content is to be added here.
+A site-directed mutagenesis study performed on the enzyme from ''Aspergillus fumigatus'' expressed as a recombinant protein in ''Escherichia coli'' showed that Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members
 == Three-dimensional structures ==
-Content is to be added here.
+No three-dimensional structure has been solved for this family.
 == Family Firsts ==
-;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
+;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <Shimosaka1996>.
-;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
+;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.
-;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
+;First catalytic nucleophile identification: Not yet identified.
-;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.
+;First general acid/base residue identification: Not yet identified.
 == References ==
 <biblio>
-#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.
+#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.
 #Cheng2000 pmid=11115392
 #Cheng2006 pmid=16330537