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Difference between revisions of "Glycoside Hydrolase Family 113"

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== Substrate specificities ==
 
== Substrate specificities ==
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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 &beta;-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 &beta;-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 &beta;- and &alpha;-mannosides.
 
 
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
 
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==

Revision as of 15:50, 21 November 2013

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH113
Clan GH-A
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/GH113.html


Substrate specificities

Only a single glycoside hydrolase of family GH113 has been characterized, intracellular ‘’Aa’’ManA 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

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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

  1. 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 | PubMed ID:18755688 [Zhang2008]
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    [pmid]