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 See a page that's out-of-date and just needs a touch-up?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.
Glycoside Hydrolase Family 127
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: ^^^Kiyotaka Fujita^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
Glycoside Hydrolase Family GH127 | |
Clan | GH-x |
Mechanism | retaining |
Active site residues | not known |
CAZy DB link | |
https://www.cazy.org/GH127.html |
Substrate specificities
This family of glycoside hydrolases contains β-L-arabinofuranosidase, which was recently established for HypBA1 from Bifidobacterium longum JCM 1217[1].
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
- This was determined with HypBA1 enzyme using the 1H-NMR and 13C-NMR spectra to identify the transglycosylation product β-Ara-OMe.
- 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
-
Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T.(2011)Characterization of a novel β-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member. J Biol Chem. 286(44), 38079-85.[1]