Glycoside Hydrolase Family 121

This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.

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

---

Glycoside Hydrolase Family GH121
Clan	none
Mechanism	retaining
Active site residues	not known
CAZy DB link
https://www.cazy.org/GH121.html

Substrate specificities

This family of glycoside hydrolases contains β-L-arabinobiosidases, as demonstrated for HypBA2 from Bifidobacterium longum JCM 1217 [1]. HypBA2 liberates the disaccharide Arafβ1-2Araf (β-Ara₂, a substrate of the GH127 β-L-arabinofuranosidase from B. longum JCM 1217 [2]) from unmodified Arafβ1-2Arafβ1-2Arafβ-hydroxyproline (Ara₃-Hyp) but not Arafα1-3Arafβ1-2Arafβ1-2Arafβ-Hyp (Ara₄-Hyp) or Arafβ1-2Arafβ-Hyp (Ara₂-Hyp). HypBA2 directly liberates β-Ara₂ from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The family members are only found from prokaryote genomes, such as bacteria and actinomycetes.

Kinetics and Mechanism

HypBA2 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol; the resulting Arafβ1-2Arafβ-Me was identified by ¹H-NMR and ¹³C-NMR analysis.

Catalytic Residues

Not known.

Three-dimensional structures

Not known.

Family Firsts

First stereochemistry determination

This was determined with HypBA2 enzyme by measurement of glycosyl transfer reactions to methanol and the ¹H-NMR and ¹³C-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, Sakamoto S, Ono Y, Wakao M, Suda Y, Kitahara K, and Suganuma T. (2011). Molecular cloning and characterization of a beta-L-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. J Biol Chem. 2011;286(7):5143-50. DOI:10.1074/jbc.M110.190512 |
2. 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 |