Reference - Detail
| RRC ID | 15607 |
|---|---|
| Author | Hirano J, Miyamoto K, Ohta H. |
| Title | Purification and characterization of thermostable H2O2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. |
| Journal | Appl Microbiol Biotechnol |
| Abstract |
A cytoplasmic NADH oxidase (NOX) was purified from a soil bacteria, Brevibacterium sp. KU1309, which is able to grow in the medium containing 2-phenylethanol as the sole source of carbon under an aerobic condition. The enzyme catalyzed the oxidation of NADH to NAD+ involving two-electron reduction of O2 to H2O2. The molecular weight of the enzyme was estimated to be 102 kDa by gel filtration and 57 kDa by SDS-PAGE, which indicates that the NOX was a homodimer consisting of a single subunit. The enzyme was stable up to 70 degrees C at a broad range of pH from 7 to 11. The enzyme activity increased about ten-fold with the addition of ammonium salt, while it was inhibited by Zn2+ (39%), Cu2+ (41%), Hg2+ (72%) and Ag+ (37%). The enzyme acts on NADH, but not on NADPH. The regeneration of NAD+ utilizing this enzyme made selective oxidation of mandelic acid or L: -phenylalanine possible. This thermostable enzyme is expected to be applicable as a useful biocatalyst for NAD+ recycling. |
| Volume | 80(1) |
| Pages | 71-8 |
| Published | 2008-8-1 |
| DOI | 10.1007/s00253-008-1535-x |
| PMID | 18521590 |
| MeSH | Amino Acid Sequence Bacterial Proteins / chemistry* Bacterial Proteins / genetics Bacterial Proteins / isolation & purification* Bacterial Proteins / metabolism Brevibacterium / chemistry Brevibacterium / enzymology* Brevibacterium / genetics Brevibacterium / metabolism Cholesterol / metabolism Enzyme Stability Hot Temperature Hydrogen Peroxide / metabolism* Kinetics Molecular Sequence Data Multienzyme Complexes / chemistry* Multienzyme Complexes / genetics Multienzyme Complexes / isolation & purification* Multienzyme Complexes / metabolism NADH, NADPH Oxidoreductases / chemistry* NADH, NADPH Oxidoreductases / genetics NADH, NADPH Oxidoreductases / isolation & purification* NADH, NADPH Oxidoreductases / metabolism Oxidation-Reduction Phenylethyl Alcohol / metabolism* Sequence Alignment Substrate Specificity |
| IF | 3.53 |
| Times Cited | 18 |
| WOS Category | BIOTECHNOLOGY & APPLIED MICROBIOLOGY |
| Resource | |
| General Microbes | JCM 20313 |