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Glycoside Hydrolase Family 44
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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, 5, 6, 6, 6, 6, 6, 6, 7, 8, 8, 9, 9, 10, 10, 11, 11, 11, 11, 12, 12, 13, 13, 14, 14, 15, 16, 16, 17, 18, 19, 19, 19, 20, 20, 21, 21, 21, 22, 23, 24, 25, 26, 26, 27, 28, 29, 30, 31, 32, 32, 33, 34, 34, 34, 35, 35, 35, 36, 36, 37, 38, 38, 38, 39, 39, 39, 39, 39, 39, 39, 40, 41, 42, 42, 43, 43, 43, 44, 45, 45, 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, 70, 71, 72, 73].
- 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.