NADPH-dependence of vitamin B2-aldehyde-forming enzyme.

Abstract

Vitamin B2-aldehyde-forming enzyme isolated from Schizophyllum commune with 1400-fold purity required NADPH under aerobic but not anaerobic conditions. NADPH- and DCIP[2,6-dichlorophenolindophenol]-requiring enzyme activities which could not be separated by an enzyme purification system were present 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[p-chloromercuribenzoate] and arsenite, inhibited the formation of vitamin B2-aldehyde to various extents, whereas azide did not.