Glycoside Hydrolase Family 12

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• Author: ^^^Mats Sandgren^^^
• Responsible Curator: ^^^Mats Sandgren^^^

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Glycoside Hydrolase Family GHnn
Clan	GH-C
Mechanism	retaining
Active site residues	known
CAZy DB link
http://www.cazy.org/fam/GH12.html

Substrate specificities

The substrate specificities found among the glycoside hydrolases of family 12 are: endo-β-1,4-glucanase (EC 3.2.1.4), xyloglucan hydrolase (EC 3.2.1.151), endo-β-1,3-1,4-glucanase (EC 3.2.1.73), and xyloglucan endo-transglycosylase (EC 2.4.1.207),.

Kinetics and Mechanism

GH Family 12 enzymes are retaining enzymes, as first shown by NMR studdies [1] on endoglucanase 3 from Humicola insolens, and follow a classical Koshland double-displacement mechanism. No detailed studies involving both steady state and pre-steady state kinetic have yet been reported for this family.

Catalytic Residues

The catalytic nucleophile of GH family 12 enzymes was initialy predicted by sequence homology to the xylanase members of GH family 11, a glycoside hydrolase family where the catalytic nucleophile was first identified in the Bacillus circulans endo-xylanase through trapping of the 2-deoxy-2-fluoroxylobiosyl-enzyme intermediate and subsequent peptide mapping via LC-MS/MS technologies [2].

Three-dimensional structures

Content is to be added here.

Family Firsts

First sterochemistry determination

Cite some reference here, with a short (1-2 sentence) explanation [3].

First catalytic nucleophile identification

Cite some reference here, with a short (1-2 sentence) explanation [4].

First general acid/base residue identification

Cite some reference here, with a short (1-2 sentence) explanation [5].

First 3-D structure

Cite some reference here, with a short (1-2 sentence) explanation [2].

References

1. Schou C, Rasmussen G, Kaltoft MB, Henrissat B, and Schülein M. (1993). Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur J Biochem. 1993;217(3):947-53. DOI:10.1111/j.1432-1033.1993.tb18325.x |
2. Miao S, Ziser L, Aebersold R, and Withers SG. (1994). Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry. Biochemistry. 1994;33(23):7027-32. DOI:10.1021/bi00189a002 |