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Difference between revisions of "Glycoside Hydrolase Family 44"
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|'''Active site residues''' | |'''Active site residues''' | ||
| − | + | ||
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
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== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. ''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 | |
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#He1999 pmid=9312086 | #He1999 pmid=9312086 | ||
#StickWilliams isbn=978-0-240-52118-3 | #StickWilliams isbn=978-0-240-52118-3 | ||
| − | #Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | + | #Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. |
| + | [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH044]] | [[Category:Glycoside Hydrolase Families|GH044]] | ||
Revision as of 12:06, 13 August 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: ^^^Peter Reilly^^^
- Responsible Curator: ^^^Peter Reilly^^^
| Glycoside Hydrolase Family GH44 | |
| Clan | None specified |
| Mechanism | Retaining |
| Active site residues
| |
| CAZy DB link | |
| http://www.cazy.org/GH44.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.
Catalytic Residues
Clostridium thermocellum: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Clostridium acetobutylicum: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352
Three-dimensional structures
Content is to be added here.
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 |
- 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.