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Difference between revisions of "Glycoside Hydrolase Family 113"
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== Substrate specificities == | == Substrate specificities == | ||
| − | Only a single [[glycoside hydrolase]] of family [[GH113]] has been characterized, intracellular | + | Only a single [[glycoside hydrolase]] of family [[GH113]] has been characterized, intracellular ''Aa''ManA from ''Alicyclobacillus acidocaldarius'' Tc-12-31 <cite>Zhang2008</cite>. This thermoacidophilic organism was originally selected for its ability to hydrolyse konjac glucomannan <cite>Zhang2008</cite>. 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) <cite>Zhang2008</cite>. No activity was observed against the other polysaccharides and ''p''-nitrophenyl glycosides tested, including ''p''-nitrophenyl β- and α-mannosides. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 14:51, 21 November 2013
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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
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
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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