In enzymology, a NADPH dehydrogenase (EC ) is an enzyme that catalyzes the chemical reaction

NADPH + H+ + acceptor ⇌ {\displaystyle \rightleftharpoons } NADP+ + reduced acceptor

The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. It has 2 cofactors: FAD, and FMN.

Nomenclature

The systematic name of this enzyme class is NADPH:acceptor oxidoreductase. Other names in common use include

  • NADPH2 diaphorase
  • NADPH diaphorase
  • old yellow enzyme
  • diaphorase
  • dihydronicotinamide adenine dinucleotide phosphate dehydrogenase
  • NADPH-dehydrogenase
  • NADPH-diaphorase
  • NADPH2-dehydrogenase
  • reduced nicotinamide adenine dinucleotide phosphate dehydrogenase
  • TPNH dehydrogenase
  • TPNH-diaphorase
  • triphosphopyridine diaphorase
  • triphosphopyridine nucleotide diaphorase
  • NADPH2 dehydrogenase
  • NADPH:(acceptor) oxidoreductase.
  • Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 477–494.
  • Avron M, Jagendorf AT (November 1957). "Some further investigations on chloroplast TPNH diaphorase". Archives of Biochemistry and Biophysics. 72 (1): 17–24. doi:. PMID .
  • Jagendorf AT (1963). [60] Chloroplast TPNH diaphorase. Methods Enzymol. Vol. 6. pp. 430–434. doi:. ISBN 978-0-12-181806-7. {{cite book}}:ISBN / Date incompatibility (help)
  • Theorell H (1935). "Das gelbe Oxydationsferment". Biochem. Z. 278: 263–290.
  • Akeson A, Theorell H (November 1956). "Molecular weight and FMN content of crystallin old yellow enzyme". Archives of Biochemistry and Biophysics. 65 (1): 439–448. doi:. PMID .
  • Boron WF, Boulpaep EL (2008). Medical Physiology.

Further reading

  • Davis EM, Ringer KL, McConkey M, Croteay R (2005). .[permanent dead link]
  • Matthijs HC, Coughlan SJ, Hind G (September 1986). . The Journal of Biological Chemistry. 261 (26): 12154–8. doi:. PMID .