NADPH dehydrogenase

From Wikipedia, the free encyclopedia

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

NADPH + H⁺ + acceptor $\rightleftharpoons$ 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. The systematic name of this enzyme class is NADPH:acceptor oxidoreductase. Other names in common use include NADPH2 diaphorase, NADPH diaphorase, OYE, 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1BWK, 1BWL, 1HDO, 1HE2, 1HE3, 1HE4, 1HE5, 1K02, 1K03, 1OYA, 1OYB, and 1OYC.

[edit] References

IUBMB entry for 1.6.99.1
BRENDA references for 1.6.99.1 (Recommended.)
PubMed references for 1.6.99.1
PubMed Central references for 1.6.99.1
Google Scholar references for 1.6.99.1
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 AT (1957). "Some further investigations on chloroplast TPNH diaphorase". Arch. Biochem. Biophys. 72: 17–24. doi:10.1016/0003-9861(57)90169-8. PMID 13471057.
Jagendorf AT (1963). "Chloroplast TPNH diaphorase". Methods Enzymol. 6: 430–434.
Theorell H (1935). "Das gelbe Oxydationsferment". Biochem. Z. 278: 263–290.
Theorell H and Akesson A (1956). "Molecular weight and FMN content of crystalline "old yellow enzyme"". Arch. Biochem. Biophys. 65: 439–448. doi:10.1016/0003-9861(56)90204-1.