RRC ID 73947
著者 Inouye S.
タイトル NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein.
ジャーナル FEBS Lett
Abstract The NAD(P)H-flavin oxidoreductase gene from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, was expressed in Escherichia coli, and the enzyme purified using Cibacron Blue 3G-A affinity column chromatography from crude extracts in a single step. The purified enzyme had a typical flavoprotein absorption spectrum and flavin mononucleotide (FMN) was identified as a prosthetic group, non-covalently bound in a molar ratio of 1:1. The enzyme catalyzed the electron transfer from NADH via FMNH2 to various other electron acceptors. Reduced flavin produced by flavin reductase participated non-enzymatically in the following reactions: H2O2-forming NADH oxidase-like, oxygen-insensitive nitroreductase-like, diaphorase (quinone reductase)-like and bacterial luciferase reactions.
巻・号 347(2-3)
ページ 163-8
公開日 1994-6-27
DOI 10.1016/0014-5793(94)00528-1
PII 0014-5793(94)00528-1
PMID 8033996
MeSH Amino Acid Sequence Chromatography, Affinity Electron Transport Electrophoresis, Polyacrylamide Gel Enzyme Stability Escherichia coli FMN Reductase Flavin Mononucleotide / analysis Flavin Mononucleotide / chemistry Flavin Mononucleotide / metabolism Hot Temperature Hydrogen Peroxide / metabolism Hydrogen-Ion Concentration Luminescence Molecular Sequence Data Molecular Weight NAD / metabolism NADH, NADPH Oxidoreductases / chemistry NADH, NADPH Oxidoreductases / genetics NADH, NADPH Oxidoreductases / metabolism* Recombinant Proteins Spectrophotometry Vibrio / enzymology*
IF 3.057
リソース情報
遺伝子材料 pJN-FRase (RDB19835)