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Difference between revisions of "Glycoside Hydrolase Family 86"
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== Catalytic Residues == | == Catalytic Residues == | ||
− | + | Actually, the catalytic residues can only be inferred from analogy to clan GH-A enzymes as two glutamate residues. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
− | + | No 3D structure is available to date. | |
Revision as of 11:34, 3 September 2010
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: ^^^Mirjam Czjzek^^^
- Responsible Curator: ^^^Mirjam Czjzek^^^
Glycoside Hydrolase Family GH86 | |
Clan | GH-A |
Mechanism | probably retaining |
Active site residues | inferred from clan GH-A as two Glu |
CAZy DB link | |
https://www.cazy.org/GH86.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
Actually, a potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan GH-A enzymes https://www.cazy.org/GH86.html. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.
Catalytic Residues
Actually, the catalytic residues can only be inferred from analogy to clan GH-A enzymes as two glutamate residues.
Three-dimensional structures
No 3D structure is available to date.
Family Firsts
- First stereochemistry 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 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006