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Difference between revisions of "Glycoside Hydrolase Family 43"

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

Revision as of 03:45, 18 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-arabinofuanose, D-galactopyranose and D-xylopyranose residues are hydrolyzed from the non-reducing end of polysacchrides or aryl groups. In addition examples of endo-alpha1,5-arabinanases are also evident in this family

Kinetics and 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]