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Difference between revisions of "Glycoside Hydrolase Family 44"
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== Catalytic Residues == | == Catalytic Residues == | ||
| − | ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 | + | ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 Kitago2007. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2009<cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010<cite>. |
Revision as of 13:59, 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
Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu | |
| 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 endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 Kitago2007. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [1, 5, 6, 6, 6, 6, 7, 7, 7, 8, 8, 9, 9, 9, 10, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 19, 20, 21, 22, 23, 24, 25, 25, 26, 27, 27, 27, 28, 28, 28, 29, 29, 30, 31, 31, 31, 32, 32, 32, 32, 32, 32, 32, 33, 34, 35, 35, 36, 36, 36, 37, 38, 38, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69].
- 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
- Kitago et al. [1] of an endoglucanase from Clostridium thermocellum. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.
References
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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.
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Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.
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Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.