Glycoside Hydrolase Family 127

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

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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.

References

1. Fujita K, Takashi Y, Obuchi E, Kitahara K, and Suganuma T. (2011). Characterization of a novel β-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member. J Biol Chem. 2011;286(44):38079-38085. DOI:10.1074/jbc.M111.248690 |