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Difference between revisions of "Glycoside Hydrolase Family 92"
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== Catalytic Residues == | == Catalytic Residues == | ||
Content is to be added here. | 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 == | == Three-dimensional structures == | ||
Revision as of 09:16, 26 October 2009
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.
- Author: ^^^Harry Gilbert^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| 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
Content is to be added here.
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
Kinetics and Mechanism
Content is to be added here. 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. [5] 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 [6].
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 [1].
- 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 [2].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
References
- 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 |
- 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 |
- Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006