title: Stereospecificity of hydride transfer and substrate specificity for FMN-containing NAD(P)H-flavin oxidoreductase from the luminescent bacterium, Vibrio fischeri ATCC 7744.
abstract: The stereospecificity of the hydride transfer in NAD(P)H-flavin reductase reaction of V. fischeri ATCC 7744 was determined by 1H-NMR spectroscopy using stereospecifically labeled reduced beta-nicotinamide adenine dinucleotide (beta-NADH). The recombinant flavoenzyme, purified from E. coli cells, selectively transferred the pro-R hydrogen at the C-4 position of the nicotinamide ring to flavin and is therefore classified as an A-side specific enzyme. Lumiflavin was used for the reductase reaction, but lumichrome and alpha-NADH were not utilized as electron acceptor and donor, respectively.
authors.affiliation: Yokohama Research Center, Chisso Corporation, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Inouye
authors.forename: H
authors.initials: H
authors.lastname: Nakamura
mesh_terms: D038181:FMN Reductase; D006859:Hydrogen / Q000378:metabolism*; D009243:NAD / Q000737:chemistry; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D014733:Vibrio / Q000201:enzymology*
chemical_list: D009243:NAD; D006859:Hydrogen; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases