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Glycoside Hydrolase Family 92

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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-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
http://www.cazy.org/fam/GHnn.html


Substrate specificities

GH92 enzymes are exo-acting alpha-mannosidases. The first reported enzyme activity from this family was an alpha1,2-mannosidase from Microbacterium sp. M-90. [1] Recently the characterization of 22 GH92 enzymes from Bacteroides thetaiotaomicron confirmed an exo-mode of action but alpha1,2-mannosidase, alpha1,3-mannosidase, alpha1,4-mannosidase and alpha1,6-mannosidase activities were detected [2] [3, 4, 5].

Kinetics and Mechanism

1H-NMR studies on three GH92s that displayed alpha1,2-, alpha1,3- and alpha1,4-mannosidase activities all generated beta-mannose indicating that these enzymes catalyse glycosidic bond hydrolysis through a single displacement mechanism leading to inversion of anomeric configuration [3, 4, 5].

Catalytic Residues

Content is to be added here. Based on 3D structural data on the alpha1,2-mannosidase Bt3990 Glu533 is the predicted catalytic acid. This view is supported by a mutant of this residue, which is essentially inactive, and its conservation throughout the GH92 family.

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 [6].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [7].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [8].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [9].

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 | PubMed ID:17323919 [Comfort2007]
  2. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [MikesClassic]
  3. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 | PubMed ID:9312086 [He1999]
  4. Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science. [3]

All Medline abstracts: PubMed