CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Glycoside Hydrolase Family 26"
Jump to navigation
Jump to search
| Line 1: | Line 1: | ||
== 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 | + | 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> and beta-1,3 xylanase activities. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 11:29, 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, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26].
- 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 |