Reference - Detail
| RRC ID | 15951 |
|---|---|
| Author | Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T. |
| Title | Characterization of a novel β-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member. |
| Journal | J Biol Chem |
| Abstract |
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-366 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. |
| Volume | 286(44) |
| Pages | 38079-38085 |
| Published | 2011-11-4 |
| DOI | 10.1074/jbc.M111.248690 |
| PII | S0021-9258(20)50650-9 |
| PMID | 21914802 |
| PMC | PMC3207453 |
| MeSH | Bifidobacterium / enzymology* Chromatography, High Pressure Liquid Fermentation Glycoside Hydrolases / chemistry* Glycosylation Hydrolysis Kinetics Models, Chemical Molecular Sequence Data Mutagenesis, Site-Directed Oligosaccharides / chemistry Polymers / chemistry Substrate Specificity Temperature Time Factors |
| IF | 4.238 |
| Times Cited | 6 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Resource | |
| General Microbes | JCM 1192 JCM 1205 JCM 1217 JCM 1222 JCM 1254 JCM 1275 JCM 7054 |