| Literature DB >> 24385433 |
Kiyotaka Fujita1, Yukari Takashi, Eriko Obuchi, Kanefumi Kitahara, Toshihiko Suganuma.
Abstract
Pfam DUF1680 (PF07944) is an uncharacterized protein family conserved in many species of bacteria, actinomycetes, fungi, and plants. Previously, 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 study provides the first characterization of a DUF1680 family member, which defines a new family of glycoside hydrolases, the glycoside hydrolase family 127.Entities:
Keywords: Bacteria; Cloning; Enzyme Catalysis; Enzyme Kinetics; Glycosidases; Hydrolases; Hydroxyproline; Mutagenesis; Protein Expression
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Year: 2014 PMID: 24385433 PMCID: PMC3931080 DOI: 10.1074/jbc.M113.528711
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157