| NADPH dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC no. | 1.6.99.1 | ||||||||
| CAS no. | 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 / 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. 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
- 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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