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Difference between revisions of "Glycoside Hydrolase Family 43"

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* [[Author]]: [[User:SatoshiKaneko|Satoshi Kaneko]]
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* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]]
* [[Responsible Curator]]:  [[User:hbrumer3|Harry Brumer]]
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* [[Responsible Curator]]:  [[User:Harry Gilbert|Harry Gilbert]]
 
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Revision as of 15:01, 19 June 2009



Glycoside Hydrolase Family GH43
Clan GH-F
Mechanism inverting
Active site residues not known
CAZy DB link
http://www.cazy.org/fam/GH43.html

Substrate specificities

GH43 enzymes display a variety of exo-activities in which L-alpha-arabinofuanose, D-beta-galactopyranose and D-beta-xylopyranose residues are hydrolyzed from the non-reducing end of polysaccharides or aryl groups. In addition examples of endo-alpha1,5-arabinanases are also evident in this family

Kinetics and Mechanism

NMR, deploying arabinan as the substrate, showed that an endo-alpha1,5-arabinanase displays a single displacement or inverting mechanism

Catalytic Residues

Three-dimensional structures

Family Firsts

First sterochemistry determination
First catalytic nucleophile identification
First general acid/base residue identification
First 3-D structure
alpha-L-Arabinanase from Cellvibrio japonicus [1].

References

  1. Nurizzo D, Turkenburg JP, Charnock SJ, Roberts SM, Dodson EJ, McKie VA, Taylor EJ, Gilbert HJ, and Davies GJ. (2002). Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nat Struct Biol. 2002;9(9):665-8. DOI:10.1038/nsb835 | PubMed ID:12198486 [1]