NADPH dehydrogenase
| NADPH dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC number | 1.6.99.1 | ||||||||
| CAS number | 9001-68-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
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, 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.
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 AT (1957). "Some further investigations on chloroplast TPNH diaphorase". Arch. Biochem. Biophys. 72 (1): 17–24. PMID 13471057. doi:10.1016/0003-9861(57)90169-8.
- 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. PMID 13373435. doi:10.1016/0003-9861(56)90204-1.
- Walter F. Boron; Emile L. Boulpaep (2008). Medical Physiology.
- ↑ 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.)
- ↑ (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