NADPH dehydrogenase

In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction

NADPH + H+ + acceptor NADP+ + reduced acceptor
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
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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
  • old yellow enzyme
  • reduced nicotinamide adenine dinucleotide phosphate dehydrogenase
  • TPNH dehydrogenase
  • TPNH-diaphorase
  • triphosphopyridine diaphorase
  • triphosphopyridine nucleotide diaphorase
  • NADPH2 dehydrogenase
  • NADPH:(acceptor) oxidoreductase.

References

    • 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). "Chloroplast TPNH diaphorase". Methods Enzymol. 6: 430–434. doi:10.1016/0076-6879(63)06200-5.
    • 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

    • Davis EM, Ringer KL, McConkey M, Croteay R (2005). "Enzyme Menthol deghydrogenase".
    • Matthijs HC, Coughlan SJ, Hind G (September 1986). "Removal of ferredoxin:NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site". The Journal of Biological Chemistry. 261 (26): 12154–8. PMID 3745183.


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