Search results for CYP3A4

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Protein (2 results from a total of 2)

Identifier: R-HSA-52639
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: CYP3A4: P08684
Identifier: R-HSA-2980797
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: CYP3A43: Q9HB55

Reaction (6 results from a total of 6)

Identifier: R-HSA-211948
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, endoplasmic reticulum lumen
The CYP3A family are the most abundantly expressed P450s in human liver, accounting for around 50% of xenobiotic drug metabolism. CYP3A4 is the most abundant member of the family and possesses broad specificity to a range of xenobiotics. Loperamide (LOP), an antidiarrheal, is mainly metabolized to desmethylloperamide (DLOP) through the N-demethylation pathway. This initial N-demethylation is carried out by CYP3A4.
Identifier: R-HSA-211959
Species: Homo sapiens
Compartment: smooth endoplasmic reticulum
CYP3A43 belongs to the cytochrome P450 3A family, of which CYP3A4 is the most active member in the biotransformation of xenobiotics. Testosterone (TEST) metabolites are a major determinant of prostate growth and differentiation. CYP3A43, which is expressed in the prostate, exhibits minor 6-beta-hydroxylation activity towards TEST suggesting CYP3A43 may be involved in the etiology of prostate cancer (Domanski et al. 2001, Zeigler-Johnson et al. 2004).
Identifier: R-HSA-213175
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, endoplasmic reticulum lumen
Aflatoxins are produced by the fungal molds Aspergillus flavus and Aspergillus parasiticus. Dietary contamination accounts for adverse health problems including liver cancer therby classifying aflatoxins as Group 1 carcinogens in humans. The B1 form of aflatoxin (AFB1) is especially carcinogenic in a number of species including humans.
AFB1 requires microsomal oxidation to produce epoxides which are the cause of their toxic and carcinogenic effects. In humans, both CYP3A4 and CYP3A5 are able to produce epoxide stereoisomers of AFB1, the most potent being aflatoxin B1 exo-8,9-oxide (AFXBO) (Gallagher et al. 1996).
Identifier: R-HSA-5423664
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
Metabolites that are formed from aflatoxin B1 (AFB1) include AFQ1, AFM1 and AFP1 (Gallagher et al. 1996). These metabolites and other naturally occurring aflatoxins (G1, B2 and G2) are poorer substrates for epoxidation and, consequently, are less mutagenic, carcinogenic and toxic than AFB1. AFB1 metabolites can be useful biomarkers of human exposure to aflatoxins and AFM1, AFQ1 and AFP1 have all been detected in human urine samples (Groopman et al. 1985). Cytochrome P450 3A4 and 3A5 are the predominant enzymes involved in AFQ1 (3-hydroxy aflatoxin) production (Raney et al. 1992).
Identifier: R-HSA-156526
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
Aflatoxin B1 (AFB1) requires microsomal oxidation to produce epoxides which cause the toxic and carcinogenic effects. In humans, cytochrome P450 enzymes produce epoxide stereoisomers of AFB1, the most potent being aflatoxin exo-8,9-oxide (AFXBO). This conversion is carried out by at least four P450s; 1A2, 3A4, 3A5 and 2A13. CYP3A4 mainly produces the exo form whereas CYP1A2 produces a racemic mixture of exo and endo forms (Gallagher et al. 1996, He et al. 2006).
Identifier: R-HSA-5423672
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
Aflatoxin B1 (AFB1) requires microsomal oxidation to produce epoxides which cause the toxic and carcinogenic effects. In humans, cytochrome P450 enzymes produce epoxide stereoisomers of AFB1, the most potent being aflatoxin exo-8,9-oxide (AFNBO). CYP3A4 and CYP1A2 can also produce aflatoxin B1-endo-8,9-epoxide (Raney et al. 1992, Ueng et al. 1995).

Set (1 results from a total of 1)

Identifier: R-HSA-5423680
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
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