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Difference between revisions of "Glycoside Hydrolase Family 26"
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== Substrate specificities == | == Substrate specificities == | ||
| − | This family consists primarily of endo-beta1,4-mannanases, although a recent exo-acting beta- mannanase has been described. The family also contains enzymes that display beta-1,3:1,4-glucanase <cite>#1<cite> and beta-1,3 xylanase activities. | + | This family consists primarily of endo-beta1,4-mannanases, although a recent exo-acting beta- mannanase has been described. The family also contains enzymes that display beta-1,3:1,4-glucanase <cite>#1</cite> and beta-1,3 xylanase activities. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 10:32, 29 June 2009
Substrate specificities
This family consists primarily of endo-beta1,4-mannanases, although a recent exo-acting beta- mannanase has been described. The family also contains enzymes that display beta-1,3:1,4-glucanase [1] and beta-1,3 xylanase activities.
Kinetics and Mechanism
Catalytic Residues
Three-dimensional structures
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short explanation [1].
- First catalytic nucleophile identification
- First general acid/base residue identification
- First 3-D structure
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 |
- Araki T, Hashikawa S, and Morishita T. (2000). Cloning, sequencing, and expression in Escherichia coli of the new gene encoding beta-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214. Appl Environ Microbiol. 2000;66(4):1741-3. DOI:10.1128/AEM.66.4.1741-1743.2000 |