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Difference between revisions of "Glycoside Hydrolase Family 44"
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== References == | == References == | ||
<biblio> | <biblio> | ||
| − | |||
#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. | #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] | [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | ||
| − | + | #Kitago2007 Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703–35711. DOI 10.1074/jbc.M706835200 | |
| − | #Kitago2007 Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH044]] | [[Category:Glycoside Hydrolase Families|GH044]] | ||
Revision as of 11:16, 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 | |
| https://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
- 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 |
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202.
-
Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703–35711. DOI 10.1074/jbc.M706835200