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Glycoside Hydrolase Family 127
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- Author: ^^^Kiyotaka Fujita^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
| Glycoside Hydrolase Family GH127 | |
| Clan | none |
| 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 activity, which was established for HypBA1 from Bifidobacterium longum JCM 1217 [1]. HypBA1 released L-arabinose from the following saccharides and amino acid glycoconjugates, but not from from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin:
- Arafβ1-2Araf (β-Ara2)
- Arafβ-hydroxyproline (Ara-Hyp)
- Arafβ1-2Arafβ-Hyp (Ara2-Hyp)
- Arafβ1-2Arafβ1-2Arafβ-hyp (Ara3-Hyp)
- methyl β-L-arabinofuranoside
- Arafβ1-2Arafβ-Me
The members of GH127 are also members of the Pfam DUF1680 family, which is conserved in many species of bacteria, actinomycetes, fungi, and plants. Establishment of GH127 by biochemical analysis thus resolves the "domain of unknown function" status of this PFAM family.
Kinetics and Mechanism
HypBA1 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol, and produced methyl β-L-arabinofuranoside was identified by 1H-NMR and 13C-NMR analysis [1].
Catalytic Residues
Not known.
Three-dimensional structures
Not known.
Family Firsts
- First stereochemistry determination
- This was determined with HypBA1 enzyme by measurement of glycosyl transfer reactions to methanol and the 1H-NMR and13C-NMR spectra [1].
- First catalytic nucleophile identification
- No experimental proof.
- First general acid/base residue identification
- No experimental proof.
- First 3-D structure
- Not known.