NADPH dehydrogenase

In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction

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
Search PMC articles PubMed articles NCBI proteins

NADPH + H⁺ + acceptor $\rightleftharpoons$ 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). [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.