Glycoside Hydrolase Family 62

• Author: Harry Gilbert
• Responsible Curator: Harry Gilbert

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Glycoside Hydrolase Family GH62
Clan	GH-F
Mechanism	assumed to be inverting
Active site residues	inferred
CAZy DB link
http://www.cazy.org/fam/GH62.html

Substrate specificities

This small family comprises an equal number of eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases that specifically cleave either alpha1,2 or alpha1,3 L-arabinofuranose side chains from xylans [1, 2]. The enzyme will not act on xylose moieties in xylan that are decorated at both O2 and O3 with an arabinose side chain. The enzyme also displays no non-specific arabinofuranosidase activity; for example it does not hydrolyse 4-nitrophenyl-alpha-L-arabinofuranose. Several of these enzymes contain cellulose #1 or xylan #2 binding CBMs.

Kinetics and Mechanism

While the catalytic mechanism of this family have not been formerly determined, likely reflecting the extremely quick rate of mutarotation displayed by arabinose, the enzyme is predicted to display a single displacement or “inverting” mechanism. This prediction is based on the location of GH62 in Clan F, the same clan occupied by GH43 (ClanF), which is an inverting family. Similarly, although the catalytic residues have not been determined using either biochemical or mutagenesis strategies, the identity of these residues is predicted from sequence homology with GH43 enzymes, given that both the catalytic mechanism and the catalytic apparatus are conserved in glycoside hydrolase families belonging to the same clan. Thus [3] predicts that the catalytic general acid and base will be a Glu and Asp, respectively, while a second Asp modulates the pKa of the general acid.

Catalytic Residues

Predicted to be an Asp (genral acid) and Glu (genral base)

Three-dimensional structures

Based on its location in Clan F GH62s are preducted to display a 5-fold beta-propeller fold

Family Firsts

First sterochemistry determination

Cite some reference here, with a short explanation [1].

First catalytic nucleophile identification

First general acid/base residue identification

First 3-D structure

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References

1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n |