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NADPH dehydrogenase

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NADPH dehydrogenase
X-ray structure of Xenobiotic Reductase A from Pseudomonas putida. PDB entry 3l5l
Identifiers
EC no.1.6.99.1
CAS no.9001-68-7
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In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction

NADPH + H+ + acceptor 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

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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.

References

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  • 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:10.1016/0003-9861(57)90169-8. PMID 13471057.
  • Jagendorf AT (1963). [60] Chloroplast TPNH diaphorase. Methods Enzymol. Vol. 6. pp. 430–434. doi:10.1016/0076-6879(63)06200-5. ISBN 978-0-12-181806-7.
  • 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:10.1016/0003-9861(56)90204-1. PMID 13373435.
  • Boron WF, Boulpaep EL (2008). Medical Physiology.

Further reading

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