NADPH dehydrogenase

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NADPH dehydrogenase
3l5l.png
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

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. 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, and NADPH:(acceptor) oxidoreductase. It has 2 cofactors: FAD, and FMN.

References[]

  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 477-494.
  • Avron M, Jagendorf A T (1957). "Some further investigations on chloroplast TPNH diaphorase". Arch. Biochem. Biophys. 72 (1): 17–24. doi:10.1016/0003-9861(57)90169-8. PMID 13471057.CS1 maint: uses authors parameter (link)
  • 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.
  • Theorell H; Akesson A (1956). "Molecular weight and FMN content of crystalline "old yellow enzyme"". Arch. Biochem. Biophys. 65 (1): 439–448. doi:10.1016/0003-9861(56)90204-1. PMID 13373435.
  • Walter F. Boron; Emile L. Boulpaep (2008). Medical Physiology.

[1] [2]


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  1. ^ Davis EM, Ringer KL, McConkey Me, Croteay R (2005)Enzyme Menthol deghydrogenase.http://mousecyc.jax.org:1555/META/NEW-IMAGE?type=ENZYME-IN-RXNDISPLAY&object=MONOMER-6721&detail-level=3 (Links to an external site.)
  2. ^ (1986). Removal of ferredoxin:NADPH+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site. Journal of Biological Chemistry. https://www.researchgate.net/publication
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