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Glycoside Hydrolase Family 62

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

Substrate specificities

This small family of glycoside hydrolases comprises an equal number of eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases that specifically cleave either α-1,2 or α-1,3-L-arabinofuranose side chains from xylans [1, 2]. The enzymes will not act on xylose moieties in xylan that are decorated at both O2 and O3 with an arabinose side chain. The GH62 enzyme from Cellvibrio japonius also displays no non-specific arabinofuranosidase activity; for example it does not hydrolyse 4-nitrophenyl α-L-arabinofuranoside. Several of these enzymes contain cellulose-[1] or xylan-[3] 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, which is an inverting family. Prior to 3D structural data the catalytic residues were 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 [4] predicts that the catalytic general acid and general 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 (general acid) and Glu (general base)

Three-dimensional structures

Based on its location in clan F, enzymes from family GH62s are predicted to display a 5-fold β-propeller fold

Family Firsts

First sterochemistry determination
No experimental proof.
First general acid residue identification
No experimental proof.
First general base residue identification
No experimental proof.
First 3-D structure
No experimental proof.

References

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  1. Error fetching PMID 2125205: [1]
  2. Error fetching PMID 14747991: [2]
  3. Error fetching PMID 9461488: [3]
  4. Error fetching PMID 9148759: [4]

All Medline abstracts: PubMed