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 See a page that's out-of-date and just needs a touch-up?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 144"
Koichi Abe (talk | contribs) |
|||
Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
− | The founding member of glycoside hydrolase family 144 is ''endo''-β-1,2-glucanase (EC3.2.1.71) from a soil bacterium ''Chitinophaga pinensis'', which hydrolize β-1,2-linked glucan to produce a wide spectrum of corresponding oligosaccharides. This family also includes a sophorohydrolase (nonreducing end), which cleaves shorter β-1,2-glucan to release sophorose (Glc-β-1,2-Glc). From sequence analysis, ''endo''-β-1,2-glucanase activity was major one. | + | The founding member of [[glycoside hydrolase]] family 144 is ''endo''-β-1,2-glucanase (EC3.2.1.71) from a soil bacterium ''Chitinophaga pinensis'', which hydrolize β-1,2-linked glucan to produce a wide spectrum of corresponding oligosaccharides. This family also includes a sophorohydrolase (nonreducing end), which cleaves shorter β-1,2-glucan to release sophorose (Glc-β-1,2-Glc). From sequence analysis, ''endo''-β-1,2-glucanase activity was major one. |
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)'' | Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)'' |
Revision as of 20:03, 11 July 2019
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: ^^^Koichi Abe^^^
- Responsible Curator: ^^^Masahiro Nakajima^^^
Glycoside Hydrolase Family GH144 | |
Clan | GH-x |
Mechanism | retaining/inverting |
Active site residues | known/not known |
CAZy DB link | |
https://www.cazy.org/GH144.html |
Substrate specificities
The founding member of glycoside hydrolase family 144 is endo-β-1,2-glucanase (EC3.2.1.71) from a soil bacterium Chitinophaga pinensis, which hydrolize β-1,2-linked glucan to produce a wide spectrum of corresponding oligosaccharides. This family also includes a sophorohydrolase (nonreducing end), which cleaves shorter β-1,2-glucan to release sophorose (Glc-β-1,2-Glc). From sequence analysis, endo-β-1,2-glucanase activity was major one.
Authors may get an idea of what to put in each field from Curator Approved Glycoside Hydrolase Families. (TIP: Right click with your mouse and open this link in a new browser window...)
In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
-
Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |