Carbohydrate Binding Module Family 65 - Revision history

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

2021-12-18T21:16:07Z

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

Elizabeth Ficko-Blean at 18:23, 2 May 2018

2018-05-02T18:23:42Z

Elizabeth Ficko-Blean at 17:41, 2 May 2018

2018-05-02T17:41:26Z

Elizabeth Ficko-Blean at 07:44, 2 May 2018

2018-05-02T07:44:12Z

Harry Brumer at 16:45, 30 April 2018

2018-04-30T16:45:01Z

Harry Brumer: fixed intrawiki links

2018-04-30T16:44:06Z

fixed intrawiki links

Ana Luis at 19:36, 29 April 2018

2018-04-29T19:36:11Z

Ana Luis at 18:52, 29 April 2018

2018-04-29T18:52:54Z

Ana Luis at 18:32, 29 April 2018

2018-04-29T18:32:40Z

Ana Luis at 18:26, 29 April 2018

2018-04-29T18:26:21Z

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

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 The CBM65B structure was obtained in complex with XXXG (Figure 1). Four tryptophans (W602, W607, W651, and W646) make extensive hydrophobic contacs with the backbone and the xylose side chains. Alanine substitution of these tryptophans abrogated cellohexaose and β-glucan recognition, confirming the important role of these aromatic residues in backbone recognition. The mutagenesis of W607, W646 also caused a substantial reduction in affinity to xyloglucan. However, only the mutation W651A abrogated binding to all ligands (xyloglucan, β-glucan and cellohexaose), confirming the key role of this residue in ligand backbone and side chain recognition <cite>Luis2013</cite>. An additional aromatic amino acid (Y685) also makes hydrophobic interactions with xylose side chains. The mechanism of ligand recognition by CBM65A and CBM65A is driven by apolar interactions with the surface of these conserved five aromatic residues (W602, W607, W651, W646 and Tyr685), where the hydrophobic interactions with the xylose side chains make a significant contribution to CBM65 binding. Indeed, this recognition of xylose side chains explains the higher affinity to xyloglucan and XXXG comparatively to undecorated β-glucans and cellotetraose, respectively <cite>Luis2013</cite>.
-The structure in complex revealed that ligand binding is also driven by polar interactions between Q110 and the glucose backbone, since the alanine substitution of this residue significantly reduce binding to β-glucan and cellohexaose <cite>Luis2013</cite>. A second polar residue (Q106), only present in CBM65A, also plays an important role in ligand recognition. The alanine mutation of Q106 abrogated cellohexaose recognition but has no impact on binding to mixed linked β-1,3/1,4-glucans (by ITC and plant cell wall labelling assays), suggesting that this residue has a key role only in cellulose recognition and that the CBM65A binding site is capable of specifically recognizing both linear β-1,4-glucans and β-1,3-b-1,4 mixed linked glucans <cite>Luis2013</cite>.
+The structure in complex revealed that ligand binding is also driven by polar interactions between Q110 and the glucose backbone, since the alanine substitution of this residue significantly reduce binding to β-glucan and cellohexaose <cite>Luis2013</cite>. A second polar residue (Q106), only present in CBM65A, also plays an important role in ligand recognition. The alanine mutation of Q106 abrogated cellohexaose recognition but has no impact on binding to mixed linked β-1,3/1,4-glucans (by ITC and plant cell wall labelling assays), suggesting that this residue has a key role only in cellulose recognition and that the CBM65A binding site is capable of specifically recognizing both linear β-1,4-glucans and β-1,3/1,4 mixed linked glucans <cite>Luis2013</cite>.
 == Functionalities ==

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

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 == Ligand specificities ==
-The founding members of family CBM65 (CBM65A and CBM65B) were identified in ''Eubacterium cellulosolvens'' endoglucanase ''Ec''Cel5A <cite>Yoda2005</cite>. This bacterial CBM family displays affinity to plant cell wall polysaccharides. Both modules CBM65A and CBM65B bind to acid swollen cellulose, β1,3/1,4 mixed linked glucans (lichenan and barley β-glucan) and decorated β1,4-glucans such as xyloglucan, hydroxyethylcellulose (HEC) and carboxymethylcellulose (CMC) <cite>Yoda2005 Luis2013</cite>. Both CBM65 modules also have weak affinity for glucomannan but there is no reports of binding to additional alfa or beta-glucans <cite>Luis2013</cite>. By isothermal titration calorimetry (ITC), CBM65A displays higher affinity for xyloglucan comparative to β1,3/1,4 mixed linked glucans and HEC. Additionally, this CBM binds with similar affinity to the oligosaccharides cellopentaose and XXXG (X comprises glucose decorated at O6 with xylose and G corresponds to undecorated glucose), the repeating unit of xyloglucan. Binding to shorter cellooligosacharides was too week to be quantified (cellotetraose) or not detectable (cellotriose) <cite>Luis2013</cite>.
+The founding members of family CBM65 (CBM65A and CBM65B) were identified in ''Eubacterium cellulosolvens'' endoglucanase ''Ec''Cel5A <cite>Yoda2005</cite>. This bacterial CBM family displays affinity to plant cell wall polysaccharides. Both modules CBM65A and CBM65B bind to acid swollen cellulose, β-1,3/1,4 mixed linked glucans (lichenan and barley β-glucan) and decorated β-1,4-glucans such as xyloglucan, hydroxyethylcellulose (HEC) and carboxymethylcellulose (CMC) <cite>Yoda2005 Luis2013</cite>. Both CBM65 modules also have weak affinity for glucomannan but there is no reports of binding to additional alpha- or beta-glucans <cite>Luis2013</cite>. By isothermal titration calorimetry (ITC), CBM65A displays higher affinity for xyloglucan comparative to β-1,3/1,4 mixed linked glucans and HEC. Additionally, this CBM binds with similar affinity to the oligosaccharides cellopentaose and XXXG (X comprises glucose decorated at O6 with xylose and G corresponds to undecorated glucose), the repeating unit of xyloglucan. Binding to shorter cellooligosacharides was too week to be quantified (cellotetraose) or not detectable (cellotriose) <cite>Luis2013</cite>.
 == Structural Features ==
-[[File:CBM65.png|thumb|300px|right|'''Figure 1. CBM65B in complex with XXXG.''' Schematic representation of CBM65B β-shandwich fold colour ramped from blue (N-terminal) to red (C-terminal), embedded in the surface representation of the protein. XXXG is shown in stick format with glucose and sylose carbons colored yellow and magenta, respectively.]]
+[[File:CBM65.png|thumb|300px|right|'''Figure 1. CBM65B in complex with XXXG.''' Schematic representation of CBM65B β-sandwich fold colour ramped from blue (N-terminal) to red (C-terminal), embedded in the surface representation of the protein. XXXG is shown in stick format with glucose and xylose carbons colored yellow and magenta, respectively.]]
-The three-dimensional structures of ''Eubacterium cellulosolvens'' CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]) solved using X-ray display a beta-sandwich fold (Figure 1) <cite>Luis2013</cite>. The ligand binding site located at the concave surface of the protein adopts a cleft-like structure typical of a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>Luis2013</cite>.
+The three-dimensional structures of ''Eubacterium cellulosolvens'' CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]), solved using X-ray crystallography, display a beta-sandwich fold (Figure 1) <cite>Luis2013</cite>. The ligand binding site located at the concave surface of the protein adopts a cleft-like structure typical of a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>Luis2013</cite>.
-The CBM65B structure was obtained in complex with XXXG (Figure 1). Four tryptophans (W602, W607, W651, and W646) make extensive hydrophobic contacs with the backbone and the xylose side chains. Alanine substitution of these tryptophans abrogated cellohexaose and β-glucan recognition, confirming the important role of these aromatic residues in backbone recognition. The mutagenesis of W607, W646 also caused a substantial reduction in affinity to xyloglucan. However, only the mutation W651A abrogated binding to all ligand (xyloglucan, β-glucan and cellohexaose), confirming the key role of this residue in subtract backbone and side chains recognition <cite>Luis2013</cite>. An additional aromatic amino acid (Y685) also makes hydrophobic interactions with xylose side chains. The mechanism of ligand recognition by CBM65A and CBM65A is driven by apolar interactions with the surface of these conserved five aromatic residues (W602, W607, W651, W646 and Tyr685), where the hydrophobic interactions with the xylose side chains make a significant contribution to CBM65 binding. Indeed, this recognition of xylose side chains explains the higher affinity to xyloglucan and XXXG comparatively to undecorated β-glucans and cellotetraose, respectively <cite>Luis2013</cite>.
+The CBM65B structure was obtained in complex with XXXG (Figure 1). Four tryptophans (W602, W607, W651, and W646) make extensive hydrophobic contacs with the backbone and the xylose side chains. Alanine substitution of these tryptophans abrogated cellohexaose and β-glucan recognition, confirming the important role of these aromatic residues in backbone recognition. The mutagenesis of W607, W646 also caused a substantial reduction in affinity to xyloglucan. However, only the mutation W651A abrogated binding to all ligands (xyloglucan, β-glucan and cellohexaose), confirming the key role of this residue in ligand backbone and side chain recognition <cite>Luis2013</cite>. An additional aromatic amino acid (Y685) also makes hydrophobic interactions with xylose side chains. The mechanism of ligand recognition by CBM65A and CBM65A is driven by apolar interactions with the surface of these conserved five aromatic residues (W602, W607, W651, W646 and Tyr685), where the hydrophobic interactions with the xylose side chains make a significant contribution to CBM65 binding. Indeed, this recognition of xylose side chains explains the higher affinity to xyloglucan and XXXG comparatively to undecorated β-glucans and cellotetraose, respectively <cite>Luis2013</cite>.
-The structure in complex revealed that the ligand biding is also driven by polar interactions between Q110 and the glucose backbone, since the alanine substitution of this residue significantly reduce binding to β-glucan and cellohexaose <cite>Luis2013</cite>. A second polar residue (Q106), only present in CBM65A, also plays an important role in ligand recognition. The alanine mutation of Q106 abrogated cellohexaose recognition but has no impact on binding to mixed linked β1,3/1,4-glucans (by ITC and plant cell wall labelling assays), suggesting that this residue has a key role only in cellulose recognition and CBM65A binding site is capable of specifically recognise both linear β1,4-glucans and β1,3-b-1,4 mixed linked glucans <cite>Luis2013</cite>.
+The structure in complex revealed that ligand binding is also driven by polar interactions between Q110 and the glucose backbone, since the alanine substitution of this residue significantly reduce binding to β-glucan and cellohexaose <cite>Luis2013</cite>. A second polar residue (Q106), only present in CBM65A, also plays an important role in ligand recognition. The alanine mutation of Q106 abrogated cellohexaose recognition but has no impact on binding to mixed linked β-1,3/1,4-glucans (by ITC and plant cell wall labelling assays), suggesting that this residue has a key role only in cellulose recognition and that the CBM65A binding site is capable of specifically recognizing both linear β-1,4-glucans and β-1,3-b-1,4 mixed linked glucans <cite>Luis2013</cite>.
 == Functionalities ==
-CBM65 modules were first identified in the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse. The molecular architecture of ''Ec''Cel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 ([[GH5]]) <cite>Yoda2005</cite>. The CBM65A and CBM65B specificity for β-glucans (β1,4 and β1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes <cite>Yoda2005</cite>. Indeed, both GH5 catalytic modules are more active on lichenan (β1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (β1,4-glucan) than in xylan. The removal of the CBM65 modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity <cite>Yoda2005</cite>.
+CBM65 modules were first identified in the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse. The molecular architecture of ''Ec''Cel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolase family 5 ([[GH5]]) <cite>Yoda2005</cite>. The CBM65A and CBM65B specificity for β-glucans (β-1,4 and β-1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes <cite>Yoda2005</cite>. Indeed, both GH5 catalytic modules are more active on lichenan (β-1,3/1,4 mixed linked glucan) and carboxymethylcellulose (β1,4-glucan) than on xylan. The removal of the CBM65 modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role in catalysis by enhancing the enzyme activity <cite>Yoda2005</cite>.
 == Family Firsts ==
-;First Identified
+;First Identified: CBM65A and CBM65B from the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse <cite>Yoda2005</cite>.
 :CBM65A and CBM65B from the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse <cite>Yoda2005</cite>.
-;First Structural Characterization
+;First Structural Characterization: The first available crystal structure and the first complex structure of a CBM65 were CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]), respectively <cite>Luis2013</cite>.
 == References ==

@@ Line 30: / Line 30: @@
 == Functionalities ==
-CBM65s were first identified in the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse. The molecular architecture of ''Ec''Cel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 ([[GH5]]) <cite>Yoda2005</cite>. The CBM65A and CBM65B specificity for β-glucans (β1,4 and β1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes <cite>Yoda2005</cite>. Indeed, both GH5s catalytic modules are more active on lichenan (β1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (β1,4-glucan) than in xylan. The removal of the CBM65s modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity <cite>Yoda2005</cite>.
+CBM65 modules were first identified in the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse. The molecular architecture of ''Ec''Cel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 ([[GH5]]) <cite>Yoda2005</cite>. The CBM65A and CBM65B specificity for β-glucans (β1,4 and β1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes <cite>Yoda2005</cite>. Indeed, both GH5 catalytic modules are more active on lichenan (β1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (β1,4-glucan) than in xylan. The removal of the CBM65 modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity <cite>Yoda2005</cite>.
 == Family Firsts ==

@@ Line 22: / Line 22: @@
 == Structural Features ==
-The three-dimensional structures of ''Eubacterium cellulosolvens'' CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]) solved using X-ray display a beta-sandwich fold <cite>Luis2013</cite>. The ligand binding site located at the concave surface of the protein adopts a cleft-like structure typical of a type B CBM  <cite>Luis2013</cite>.
+The three-dimensional structures of ''Eubacterium cellulosolvens'' CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]) solved using X-ray display a beta-sandwich fold <cite>Luis2013</cite>. The ligand binding site located at the concave surface of the protein adopts a cleft-like structure typical of a [https://www.cazypedia.org/index.php/Carbohydrate-binding_modules type B] CBM <cite>Luis2013</cite>.
-The CBM65B structure was obtained in complex with XXXG. Four tryptophans (W602, W607, W651, and W646) make extensive hydrophobic contacs with the backbone and the xylose side chains. Alanine substitution of these tryptophans abrogated cellohexaose and b-glucan recognition, confirming the important role of these aromatic residues in backbone recognition. The mutagenesis of W607, W646 also caused a substantial reduction in affinity to xyloglucan, However, only the mutation W651A abrogated binding to all ligand (xyloglucan, b-glucan and cellohexaose), confirming the key role of this residue in subtract backbone and side chains recognition. An additional aromatic amino acid (Y685) also makes hydrophobic interactions with xylose side chains. The mechanism of ligand recognition by CBM65A and CBM65A is driven by apolar interactions with the surface of these conserved five aromatic residues (W602, W607, W651, W646 and Tyr685), where the hydrophobic interactions with the xylose side chains make a significant contribution to CBM65 binding. Indeed, this recognition of xylose side chains explains the higher affinity to xyloglucan and XXXG comparatively to undecorated b-glucans and cellotetraose, respectively.
+The CBM65B structure was obtained in complex with XXXG. Four tryptophans (W602, W607, W651, and W646) make extensive hydrophobic contacs with the backbone and the xylose side chains. Alanine substitution of these tryptophans abrogated cellohexaose and β-glucan recognition, confirming the important role of these aromatic residues in backbone recognition. The mutagenesis of W607, W646 also caused a substantial reduction in affinity to xyloglucan. However, only the mutation W651A abrogated binding to all ligand (xyloglucan, β-glucan and cellohexaose), confirming the key role of this residue in subtract backbone and side chains recognition <cite>Luis2013</cite>. An additional aromatic amino acid (Y685) also makes hydrophobic interactions with xylose side chains. The mechanism of ligand recognition by CBM65A and CBM65A is driven by apolar interactions with the surface of these conserved five aromatic residues (W602, W607, W651, W646 and Tyr685), where the hydrophobic interactions with the xylose side chains make a significant contribution to CBM65 binding. Indeed, this recognition of xylose side chains explains the higher affinity to xyloglucan and XXXG comparatively to undecorated β-glucans and cellotetraose, respectively <cite>Luis2013</cite>.
 == Functionalities ==
-CBM65s were first identified in the Eubacterium cellulosolvens EcCel5A endoglucanse. The molecular architecture of EcCel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 (GH5 page). The CBM65A and CBM65B specificity for b-glucans (b1,4 and b1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes. Indeed, both GH5s catalytic modules are more active on lichenan (b1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (b1,4-glucan) than in xylan. The removal of the CBM65s modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity.
+CBM65s were first identified in the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse. The molecular architecture of ''Ec''Cel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 ([https://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_5 GH5]) <cite>Yoda2005</cite>. The CBM65A and CBM65B specificity for β-glucans (β1,4 and β1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes <cite>Yoda2005</cite>. Indeed, both GH5s catalytic modules are more active on lichenan (β1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (β1,4-glucan) than in xylan. The removal of the CBM65s modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity <cite>Yoda2005</cite>.
 == Family Firsts ==
 ;First Identified
-:Insert archetype here, possibly including ''very brief'' synopsis.
+:CBM65A and CBM65B from the ''Eubacterium cellulosolvens'' ''Ec''Cel5A endoglucanse <cite>Yoda2005</cite>.
 ;First Structural Characterization
-:Insert archetype here, possibly including ''very brief'' synopsis.
+:The first available crystal structure and the first complex structure of a CBM65 were CBM65A ([{{PDBlink}}4AFM 4AFM]) and CBM65B ([{{PDBlink}}2YPJ 2YPJ]), respectively <cite>Luis2013</cite>.
 == References ==

@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
+The founding members of family CBM65 (CBM65A and CBM65B) were identified in ''Eubacterium cellulosolvens'' endoglucanase ''Ec''Cel5A <cite>Yoda2005</cite>. This bacterial CBM family displays affinity to plant cell wall polysaccharides. Both modules CBM65A and CBM65B bind to acid swollen cellulose, β1,3/1,4 mixed linked glucans (lichenan and barley β-glucan) and decorated β1,4-glucans such as xyloglucan, hydroxyethylcellulose (HEC) and carboxymethylcellulose (CMC)<cite>Yoda2005 Luis2013</cite>. Both CBM65 modules also have weak affinity for glucomannan but there is no reports of binding to additional alfa or beta-glucans <cite>Luis2013</cite>. By isothermal titration calorimetry (ITC), CBM65A displays higher affinity for xyloglucan comparative to β1,3/1,4 mixed linked glucans and HEC. Additionally, this CBM binds with similar affinity to the oligosaccharides cellopentaose and XXXG (X comprises glucose decorated at O6 with xylose and G corresponds to undecorated glucose), the repeating unit of xyloglucan. Binding to shorter cellooligosacharides was too week to be quantified (cellotetraose) or not detectable (cellotriose) <cite>Luis2013</cite>.
 == Structural Features ==
-''Content in this section should include, in paragraph form, a description of:''
+The three-dimensional structures of Eubacterium cellulosolvens CBM65A (4afm) and CBM65B (2ypj) solved using X-ray display a beta-sandwich fold. The ligand binding site located at the concave surface of the protein adopts a cleft-like structure typical of a type B CBM (link to CBM page).
 == Functionalities ==
-''Content in this section should include, in paragraph form, a description of:''
+CBM65s were first identified in the Eubacterium cellulosolvens EcCel5A endoglucanse. The molecular architecture of EcCel5A shows two CBM65 modules (denominated A and B) appended to two glycoside hydrolases family 5 (GH5 page). The CBM65A and CBM65B specificity for b-glucans (b1,4 and b1,3/14-mixed linked) is consistent with the reported activity of the appended enzymes. Indeed, both GH5s catalytic modules are more active on lichenan (b1,3-b-1,4 mixed linked glucan) and carboxymethylcellulose (b1,4-glucan) than in xylan. The removal of the CBM65s modules associated with the GH5 catalytic domains resulted in a significant decrease of the enzymatic activity against all tested substrates, suggesting that both binding modules have an important role on catalysis enhancing the enzyme activity.
 == Family Firsts ==
@@ Line 42: / Line 38: @@
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#Yoda2005 pmid=16204489
-#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
+#Luis2013 pmid=23229556
-#Boraston2004 pmid=15214846
 </biblio>
 [[Category:Carbohydrate Binding Module Families|CBM065]]