Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | a drug-induced enzyme | Homo sapiens |
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 | Comment | Organism | Structure |
---|---|---|---|
cimetidine | specific inhibition | Homo sapiens | |
Emulgen | a detergent that inactivates the enzyme at high concentrations | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Homo sapiens | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
More | structure-function relationship | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Cyp | - |
Homo sapiens |
CYP3A4 | - |
Homo sapiens |
cytochrome P450 monooxygenase | - |
Homo sapiens |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
inactive at pH 8.49.4 | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | - |
Homo sapiens | |
NADPH | dependent on | Homo sapiens |