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Glycoside Hydrolase Family 113
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- Author: ^^^Rohan Williams^^^ ^^^Spencer Williams^^^
- Responsible Curator: ^^^Spencer Williams^^^
| Glycoside Hydrolase Family GH113 | |
| Clan | GH-A |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH113.html | |
Substrate specificities
Only a single glycoside hydrolase of family GH113 has been characterized, intracellular AaManA from Alicyclobacillus acidocaldarius Tc-12-31 [1]. This thermoacidophilic organism was originally selected for its ability to hydrolyse konjac glucomannan [1]. The recombinantly-expressed enzyme possessed activity against polysaccharides containing β-1,4-mannosidic linkages, including significant activity against konjac glucomannan, and galactomannan from locust bean gum. Some activity was also observed against crystalline ivory nut mannan (an unsubstituted β-1,4-mannan) and guar gum (a more highly-substituted galactomannan) [1]. No activity was observed against the other polysaccharides and p-nitrophenyl glycosides tested, including p-nitrophenyl β- and α-mannosides.
Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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References
- Zhang Y, Ju J, Peng H, Gao F, Zhou C, Zeng Y, Xue Y, Li Y, Henrissat B, Gao GF, and Ma Y. (2008). Biochemical and structural characterization of the intracellular mannanase AaManA of Alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan GH-A. J Biol Chem. 2008;283(46):31551-8. DOI:10.1074/jbc.M803409200 |
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