Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 7, Pages 5143-5150Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.190512
Keywords
-
Categories
Funding
- Japan Society for the Promotion of Science [22780094]
- Grants-in-Aid for Scientific Research [22780094] Funding Source: KAKEN
Ask authors/readers for more resources
Extensin is a glycoprotein that is rich in hydroxyprolines linked to beta-L-arabinofuranosides. In this study, we cloned a hypBA2 gene that encodes a novel beta-L-arabinobiosidase from Bifidobacterium longum JCM 1217. This enzyme does not have any sequence similarity with other glycoside hydrolase families but has 38-98% identity to hypothetical proteins in Bifidobacterium and Xanthomonas strains. The recombinant enzyme liberated L-arabinofuranose (Araf)-beta 1,2-Araf disaccharide from carrot extensin, potato lectin, and Araf-beta 1,2-Araf-beta 1,2-Araf-beta-Hyp (Ara(3)-Hyp) but not Araf-alpha 1,3-Araf-beta 1,2-Araf-beta 1,2-Araf-beta-Hyp (Ara(4)-Hyp) or Araf-beta 1,2-Araf-beta-Hyp (Ara(2)-Hyp), which indicated that it was specific for unmodified Ara(3)-Hyp substrate. The enzyme also transglycosylated 1-alkanols with retention of the anomeric configuration. This is the first report of an enzyme that hydrolyzes Hyplinked beta-L-arabinofuranosides, which defines a new family of glycoside hydrolases, glycoside hydrolase family 121.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available