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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. NADPH-dependence of vitamin B2-aldehyde-forming enzyme. Tachibana, S., Oka, M. J. Nutr. Sci. Vitaminol. (1982) [Pubmed]
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