BIOMAT Database Logo BIOMAT Database Logo

Aflatoxin B1 oxidation by human cytochrome P450s. 1998

Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
National Research Institute of Chinese Medicine, Taipei, Taiwan, R.O.C.

UI MeSH Term Description Entries
D009153 Mutagens Chemical agents that increase the rate of genetic mutation by interfering with the function of nucleic acids. A clastogen is a specific mutagen that causes breaks in chromosomes. Clastogen,Clastogens,Genotoxin,Genotoxins,Mutagen
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D002273 Carcinogens Substances that increase the risk of NEOPLASMS in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included. Carcinogen,Oncogen,Oncogens,Tumor Initiator,Tumor Initiators,Tumor Promoter,Tumor Promoters,Initiator, Tumor,Initiators, Tumor,Promoter, Tumor,Promoters, Tumor
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001571 Benzoflavones Organic compounds containing a BENZENE ring attached to a flavone group. Some of these are potent arylhydrocarbon hydroxylase inhibitors. They may also inhibit the binding of NUCLEIC ACIDS to BENZOPYRENES and related compounds. The designation includes all isomers; the 7,8-isomer is most frequently encountered. Benzoflavone Compounds,Compounds, Benzoflavone
D016604 Aflatoxin B1 A potent hepatotoxic and hepatocarcinogenic mycotoxin produced by the Aspergillus flavus group of fungi. It is also mutagenic, teratogenic, and causes immunosuppression in animals. It is found as a contaminant in peanuts, cottonseed meal, corn, and other grains. The mycotoxin requires epoxidation to aflatoxin B1 2,3-oxide for activation. Microsomal monooxygenases biotransform the toxin to the less toxic metabolites aflatoxin M1 and Q1. Aflatoxin B(1),Aflatoxin B,Aflatoxin B1 Dihydrochloride, (6aR-cis)-Isomer,Aflatoxin B1, (6aR-cis)-Isomer, 14C-Labeled,Aflatoxin B1, (6aR-cis)-Isomer, 2H-Labeled,Aflatoxin B1, (6aR-cis)-Isomer, 3H-Labeled,Aflatoxin B1, cis(+,-)-Isomer,HSDB-3453,NSC-529592,HSDB 3453,HSDB3453,NSC 529592,NSC529592

Related Publications

Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Mutagenic activation of aflatoxin B1 by pulmonary, renal, and hepatic cytochrome P450s from rats.
October 1992, Mutation research,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Oxidation of 2,6-dimethylaniline by recombinant human cytochrome P450s and human liver microsomes.
June 2001, Chemical research in toxicology,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Induction of specific cytochrome P450s involved in aflatoxin B1 metabolism in hepatitis B virus transgenic mice.
October 1994, Molecular carcinogenesis,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Stereoselectivity in the oxidation of bufuralol, a chiral substrate, by human cytochrome P450s.
May 2003, Chirality,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Differential inhibition of aflatoxin B1 oxidation by gestodene action on human liver microsomes.
November 1997, Biochemistry and molecular biology international,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Bioactivation of aflatoxin B1 by human liver microsomes: role of cytochrome P450 IIIA enzymes.
May 1991, Toxicology and applied pharmacology,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
[Microsomal and photochemical oxidation of aflatoxin B1].
January 1985, Eksperimental'naia onkologiia,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
DNA recombination induced by aflatoxin B1 activated by cytochrome P450 1A enzymes.
December 1994, Molecular carcinogenesis,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Induction of cytochrome P450s by rutaecarpine and metabolism of rutaecarpine by cytochrome P450s.
August 2004, Planta medica,
Y F Ueng, and T Shimada, and H Yamazaki, and F Peterguengerich
Automated definition of the enzymology of drug oxidation by the major human drug metabolizing cytochrome P450s.
November 2000, Drug metabolism and disposition: the biological fate of chemicals,
Copied contents to your clipboard!