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Glycoside Hydrolase Family 12

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


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]. GH family 11 and 12 form together GH clan C of related GH families. The predicted catalytic nucleophile was subsequentialy confirmed through


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 [6].

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 | PubMed ID:8223652 [1]
  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 | PubMed ID:7911679 [3]

All Medline abstracts: PubMed