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Literature summary for 1.14.14.1 extracted from

  • Cashman, J.R.
    Some distinctions between flavin-containing and cytochrome P450 monooxygenases (2005), Biochem. Biophys. Res. Commun., 338, 599-604.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information a drug-induced enzyme Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information genetic variations, substantial effects of single nucleotide polymorphisms, e.g. CYP2D6 and CYP2C19 SNPs show large e.ects on metabolism of debrisoquine and (S)-mephenytoin, respectively, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
cimetidine specific inhibition Homo sapiens
Emulgen a detergent that inactivates the enzyme at high concentrations Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O catalytic reaction mechanism, structure-function relationship, CYP can oxidize non-nucleophilic substrates, CYP possesses genetic variability that may contribute to inter-individual variability observed for drug metabolism, the first step of CYP is the addition of substrate to the enzyme followed by electron transfer from the flavoprotein NADPH-CYP reductase to the substrate-bound CYP, then electrons flow to the FMN prosthetic group and then sequentially to the CYP to ultimately afford a reactive iron-oxo species, although other peroxy forms of the hemoprotein are proposed also to be oxidants involved in CYP-dependent metabolism Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-nicotine + [reduced NADPH-hemoprotein reductase] + O2 substrate of CYP3A4, the reaction involves electron transfer via FMN Homo sapiens ?
-
?
dimethylaniline + [reduced NADPH-hemoprotein reductase] + O2 substrate of CYP3A4 Homo sapiens ?
-
?
additional information in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions Homo sapiens ?
-
?
additional information CYP mainly catalyzes C-H abstraction but also oxidizes nitrogen- and sulfur-containing compounds and generally converts lipophilic compounds into more hydrophilic metabolites Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More structure-function relationship Homo sapiens

Synonyms

Synonyms Comment Organism
Cyp
-
Homo sapiens
CYP3A4
-
Homo sapiens
cytochrome P450 monooxygenase
-
Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
in absence of NADPH, the enzyme retains about 85% of the CYP functional activity Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
inactive at pH 8.4–9.4 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FMN
-
Homo sapiens
NADPH dependent on Homo sapiens