| 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 | |||||||||
| 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 | ||||||||
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In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction
- NADPH + H + acceptor NADP + reduced acceptor
NADP + reduced acceptorThe 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). [60] Chloroplast TPNH diaphorase. Methods Enzymol. Vol. 6. pp. 430–434. doi:10.1016/0076-6879(63)06200-5. ISBN 978-0-12-181806-7.
- 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. doi:10.1016/S0021-9258(18)67216-3. PMID 3745183.
| Oxidoreductases: NADH or NADPH (EC 1.6) | |
|---|---|
| 1.6.1: NAD/NADP | |
| 1.6.2: Heme | |
| 1.6.3: Oxygen | |
| 1.6.5: Quinone or similar | |
| 1.6.6: Nitrogenous group | |
| 1.6.99: other | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
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