NADPH—hemoprotein reductase

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In enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction

NADPH—hemoprotein reductase
NADPH-Cytochrome P450 reductase dimer, Rattus norvegicus
Identifiers
EC no.1.6.2.4
CAS no.9023-03-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
NADPH + H+ + n oxidized hemoprotein NADP+ + n reduced hemoprotein

The three substrates of this enzyme are NADPH, H+, and oxidized hemoprotein, whereas its two products are NADP+ and reduced hemoprotein. It has two cofactors: flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN).

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH:hemoprotein oxidoreductase. Other names include cytochrome P450 reductase, ferrihemoprotein P-450 reductase, and NADPH-dependent cytochrome c reductase.

Structural studies

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As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1AMO, 1B1C, 1J9Z, 1JA0, 1JA1, 1YQO, 1YQP, 2BF4, 2BN4, and 2BPO.

References

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