Glycoside Hydrolase Family 127

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• Author: ^^^Kiyotaka Fujita^^^
• Responsible Curator: ^^^Shinya Fushinobu^^^

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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]. The enzymes belonging to this family are also members of Pfam DUF1680 family, conserved in many species of bacteria, actinomycetes, fugi, and plants.

Kinetics and Mechanism

HypBA1 is a retaining enzyme.The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, and following 1H and 13C NMR analysis of the methanol-adducted transglycosylation product.

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.

First catalytic nucleophile identification

No experimental proof.

First general acid/base residue identification

No experimental proof.

First 3-D structure

Not known.

References

1. 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]