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Literature summary extracted from

  • Flueck, C.E.; Mullis, P.E.; Pandey, A.V.
    Reduction in hepatic drug metabolizing CYP3A4 activities caused by P450 oxidoreductase mutations identified in patients with disordered steroid metabolism (2010), Biochem. Biophys. Res. Commun., 401, 149-153.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.1 NADPH-P450 reductase supports the CYP3A4 activity through providing NADPH, mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.1 recombinant expression in Escherichia coli Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.1 Fe2+ heme protein Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.1 quinine + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions 3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.1 recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration to homogeneity Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.1 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.1 quinine + [reduced NADPH-hemoprotein reductase] + O2
-
 Homo sapiens 3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.1 quinine + [reduced NADPH-hemoprotein reductase] + O2 in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions Homo sapiens 3-hydroxyquinine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.1 CYP3A4
-
 Homo sapiens
1.14.14.1 cytochrome P450 3A4
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.1 FMN the heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions Homo sapiens
1.14.14.1 heme the heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions Homo sapiens
1.14.14.1 NADPH required, supplied by the NADPH-P450 reductase Homo sapiens

Expression

EC Number Organism Comment Expression
1.14.14.1 Homo sapiens mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity down

General Information

EC Number General Information Comment Organism
1.14.14.1 additional information loss of CYP3A4 activity may result in increased risk of drug toxicities and adverse drug reactions in patients with NADPH-P450 reductase mutations Homo sapiens