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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. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352. | + | ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3]. |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a | + | The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a ''Clostridium acetobutylicum'' endoglucanase. |
Revision as of 12:24, 13 August 2010
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- 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 | |
| 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 endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].Clostridium acetobutylicum endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].
Three-dimensional structures
The first three-dimensional structure was by Kitago et al. [1] on a Clostridium thermocellum endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a Clostridium acetobutylicum endoglucanase.
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
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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.