NADPH dehydrogenase
{{infobox enzyme
| Name = NADPH dehydrogenase
| EC_number = 1.6.99.1
| CAS_number = 9001-68-7
| GO_code = 0003959
| image = 3l5l.png
| width =
| caption = X-ray structure of Xenobiotic Reductase A from Pseudomonas putida. PDB entry {{PDBe|3l5l}}
}}
In enzymology, a NADPH dehydrogenase ({{EC number|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
{{div col|colwidth=20em}}
- 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.
{{Div col end}}
References
{{reflist|1}}
{{refbegin}}
- {{cite book | veditors = Boyer PD, Lardy H, Myrback K | title = The Enzymes | edition = 2nd | volume = 7 | publisher = Academic Press | location = New York | date = 1963 | pages = 477–494 }}
- {{cite journal | vauthors = Avron M, Jagendorf AT | title = Some further investigations on chloroplast TPNH diaphorase | journal = Archives of Biochemistry and Biophysics | volume = 72 | issue = 1 | pages = 17–24 | date = November 1957 | pmid = 13471057 | doi = 10.1016/0003-9861(57)90169-8 }}
- {{cite book | vauthors = Jagendorf AT | year = 1963 | title = [60] Chloroplast TPNH diaphorase | series = Methods Enzymol. | volume = 6 | pages = 430–434 | doi=10.1016/0076-6879(63)06200-5| isbn = 978-0-12-181806-7 }}
- {{cite journal | vauthors = Theorell H | year = 1935 | title = Das gelbe Oxydationsferment | journal = Biochem. Z. | volume = 278 | pages = 263–290 }}
- {{cite journal | vauthors = Akeson A, Theorell H | title = Molecular weight and FMN content of crystallin old yellow enzyme | journal = Archives of Biochemistry and Biophysics | volume = 65 | issue = 1 | pages = 439–448 | date = November 1956 | pmid = 13373435 | doi = 10.1016/0003-9861(56)90204-1 }}
- {{cite book | vauthors = Boron WF, Boulpaep EL | year = 2008 | title = Medical Physiology}}
{{refend}}
Further reading
{{refbegin}}
- {{cite web | vauthors = Davis EM, Ringer KL, McConkey M, Croteay R | date = 2005 | title = Enzyme Menthol deghydrogenase | url = http://mousecyc.jax.org:1555/META/NEW-IMAGE?type=ENZYME-IN-RXNDISPLAY&object=MONOMER-6721&detail-level=3 }}
- {{cite journal | vauthors = Matthijs HC, Coughlan SJ, Hind G | title = Removal of ferredoxin:NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site | journal = The Journal of Biological Chemistry | volume = 261 | issue = 26 | pages = 12154–8 | date = September 1986 | pmid = 3745183 | doi = 10.1016/S0021-9258(18)67216-3| doi-access = free | url = }}
{{refend}}
{{NADH or NADPH oxidoreductases}}
{{Enzymes}}
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Category:NADPH-dependent enzymes
Category:Enzymes of known structure
{{1.6-enzyme-stub}}