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Difference between revisions of "Glycoside Hydrolase Family 131"
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| − | * [[Author]]: | + | * [[Author]]: [[User:Jean-Guy Berrin|Jean-Guy Berrin]] |
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== Substrate specificities == | == Substrate specificities == | ||
| − | This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain cellulose-binding | + | This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family [{{CAZyDBlink}}CBM1.html CBM1]. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme | + | The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an ''exo''-mode on the non-reducing end of gluco-oligosaccharides. |
== Catalytic Residues == | == Catalytic Residues == | ||
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== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold. | |
== Family Firsts == | == Family Firsts == | ||
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;First catalytic nucleophile identification: No experimental proof. | ;First catalytic nucleophile identification: No experimental proof. | ||
;First general acid/base residue identification: No experimental proof. | ;First general acid/base residue identification: No experimental proof. | ||
| − | ;First 3-D structure: | + | ;First 3-D structure: ''Coprinopsis cinerea'' CcGH131A <cite>Miyazaki2013</cite>. |
== References == | == References == | ||
<biblio> | <biblio> | ||
#Lafond2012 pmid=23023747 | #Lafond2012 pmid=23023747 | ||
| + | #Miyazaki2013 pmid=23711369 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH131]] | [[Category:Glycoside Hydrolase Families|GH131]] | ||
Latest revision as of 13:19, 18 December 2021
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| Glycoside Hydrolase Family GH131 | |
| Clan | GH-x |
| Mechanism | not known |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH131.html | |
Substrate specificities
This family of glycoside hydrolases comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family CBM1. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete Podospora anserina [1]. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity [1].
Kinetics and Mechanism
The Podospora anserina GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives [1]. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an exo-mode on the non-reducing end of gluco-oligosaccharides.
Catalytic Residues
Not known.
Three-dimensional structures
Only one crystal structure of a glycoside hydrolase family 131 protein from Coprinopsis cinerea is available [2]. The structure of CcGH131A was found to be composed of a β-jelly roll fold.
Family Firsts
- First stereochemistry determination
- No experimental proof.
- First catalytic nucleophile identification
- No experimental proof.
- First general acid/base residue identification
- No experimental proof.
- First 3-D structure
- Coprinopsis cinerea CcGH131A [2].
References
- Lafond M, Navarro D, Haon M, Couturier M, and Berrin JG. (2012). Characterization of a broad-specificity β-glucanase acting on β-(1,3)-, β-(1,4)-, and β-(1,6)-glucans that defines a new glycoside hydrolase family. Appl Environ Microbiol. 2012;78(24):8540-6. DOI:10.1128/AEM.02572-12 |
- Miyazaki T, Yoshida M, Tamura M, Tanaka Y, Umezawa K, Nishikawa A, and Tonozuka T. (2013). Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea. FEBS Lett. 2013;587(14):2193-8. DOI:10.1016/j.febslet.2013.05.041 |