NADPH-dependence of vitamin B2-aldehyde-forming enzyme.
Vitamin B2-aldehyde-forming enzyme isolated from Schizophyllum commune with 1,400-fold purity was found to require NADPH under aerobic but not anaerobic conditions. Both NADPH- and DCIP-requiring enzyme activities which could not be separated by our enzyme purification system were found in the same single protein band on polyacrylamide disc gel electrophoresis. The cation, Cu2+, markedly stimulated the NADPH-dependent enzyme reaction under the aerobic conditions. The reagents, EDTA, pyrazole, N-ethylmaleimide, PCMB, and arsenite, inhibited the formation of vitamin B2-aldehyde to various extents, whereas azide did not.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D009249:NADP / Q000378:metabolism*; D010100:Oxygen / Q000494:pharmacology; D012256:Riboflavin / Q000031:analogs & derivatives / Q000096:biosynthesis
D008670:Metals; D009249:NADP; C023849:vitamin B2 aldehyde; D000429:Alcohol Oxidoreductases; C029140:vitamin B2-aldehyde-forming enzyme; D010100:Oxygen; D012256:Riboflavin