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NADPH dehydrogenase
From Wikipedia, the free encyclopedia
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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
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.
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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.
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References
Further reading
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