Stereochemical studies of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii.
The purified 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii catalyzes an oxidation-reduction reaction between a novel 8-hydroxy-5-deazaflavin cofactor and nicotinamide adenine dinucleotide phosphate. The reaction was shown to be a direct hydride transfer process. Using stereospecifically 3H-labeled substrates, the steric course of this process was established to be S-specific with respect to the nicotinamide nucleotide. The 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from M. vannielii and the hydrogenase system in the cell-free extracts of Methanobacterium thermoautotrophicum recognize the same side, designated as A side, with respect to the prochiral center at C-5 of the dihydro-8-hydroxy-5-deazaflavin cofactor.
D019605:Euryarchaeota / Q000201:enzymology*; D005415:Flavins / Q000494:pharmacology*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D012256:Riboflavin / Q000031:analogs & derivatives*; D013237:Stereoisomerism; D013379:Substrate Specificity; D014316:Tritium
D005415:Flavins; D014316:Tritium; C007701:factor 420; D009247:NADH, NADPH Oxidoreductases; D012256:Riboflavin