Biology:NADPH dehydrogenase

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NADPH dehydrogenase
3l5l.png
X-ray structure of Xenobiotic Reductase A from Pseudomonas putida. PDB entry 3l5l
Identifiers
EC number1.6.99.1
CAS number9001-68-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

NADPH + H+ + acceptor [math]\displaystyle{ \rightleftharpoons }[/math] 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
  • old yellow enzyme
  • reduced nicotinamide adenine dinucleotide phosphate dehydrogenase
  • TPNH dehydrogenase
  • TPNH-diaphorase
  • triphosphopyridine diaphorase
  • triphosphopyridine nucleotide diaphorase
  • NADPH2 dehydrogenase
  • NADPH:(acceptor) oxidoreductase.


References

  • The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 477–494. 
  • "Some further investigations on chloroplast TPNH diaphorase". Archives of Biochemistry and Biophysics 72 (1): 17–24. November 1957. doi:10.1016/0003-9861(57)90169-8. PMID 13471057. 
  • "Chloroplast TPNH diaphorase". Methods Enzymol. 6: 430–434. 1963. doi:10.1016/0076-6879(63)06200-5. 
  • "Das gelbe Oxydationsferment". Biochem. Z. 278: 263–290. 1935. 
  • "Molecular weight and FMN content of crystallin old yellow enzyme". Archives of Biochemistry and Biophysics 65 (1): 439–448. November 1956. doi:10.1016/0003-9861(56)90204-1. PMID 13373435. 
  • Medical Physiology. 2008. 

Further reading