Characterization of a novel {beta}-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 family member [Glycobiology and Extracellular Matrices]

January 2nd, 2014 by Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K., Suganuma, T.

Pfam DUF1680 (PF07944) is an uncharacterized protein family conserved in many species of bacteria, actinomycetes, fungi, and plants. In a previous article, we cloned and characterized the hypBA2 gene as a β-L-arabinobiosidase in Bifidobacterium longum JCM 1217. In this study, we cloned a DUF1680 family member, the hypBA1 gene, which constitutes a gene cluster with hypBA2. HypBA1 is a novel β-L-arabinofuranosidase that liberates L-arabinose from the L-arabinofuranose (Araf)-β1,2-Araf disaccharide. HypBA1 also transglycosylates 1-alkanols with retention of the anomeric configuration. Mutagenesis and azide rescue experiments indicated that Glu-338 is a critical residue for catalytic activity. This report provides the first characterization of a DUF1680 family member, which defines a new family of glycoside hydrolases, the GH family 127.
  • Posted in Journal of Biological Chemistry, Publications
  • Comments Off on Characterization of a novel {beta}-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 family member [Glycobiology and Extracellular Matrices]