Aflatoxin B1 metabolism (WP699)
Homo sapiens
'''Aflatoxins''' are naturally occurring [[wikipedia:mycotoxin|mycotoxin]]s that are produced by many species of ''[[wikipedia:Aspergillus|Aspergillus]]'', a [[wikipedia:fungus|fungus]], most notably ''[[wikipedia:Aspergillus flavus|Aspergillus flavus]]'' and ''[[wikipedia:Aspergillus parasiticus|Aspergillus parasiticus]]''. After entering the body, aflatoxins are metabolized by the liver to a reactive intermediate, aflatoxin M1, an [[wikipedia:epoxide|epoxide]]. Aflatoxin B1 is considered the most toxic and is produced by both Aspergillus flavus and Aspergillus parasiticus. Source: [[wikipedia:Aflatoxin|Wikipedia]] Proteins on this pathway have targeted assays available via the [https://assays.cancer.gov/available_assays?wp_id=WP699 CPTAC Assay Portal]
Authors
Pieter Giesbertz , Alex Pico , Thomas Kelder , Martijn Van Iersel , Christine Chichester , Martina Summer-Kutmon , Denise Slenter , Egon Willighagen , Kristina Hanspers , and Eric WeitzActivity
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Cited In
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Organisms
Homo sapiensCommunities
Annotations
Pathway Ontology
cellular detoxification pathway xenobiotic metabolic pathway aflatoxin metabolic pathwayDisease Ontology
cancerLabel | Type | Compact URI | Comment |
---|---|---|---|
Aflatoxin B1 exo-8,9-epoxide-GSH | Metabolite | pubchem.compound:5486953 | |
Aflatoxin B1 8,9-dihydrodiol | Metabolite | chebi:53106 | |
Aflatoxin B1 dialdehyde | Metabolite | chebi:53107 | |
aflatoxin B1 | Metabolite | hmdb:HMDB0006552 | |
Aflatoxin B1 exo-8,9-epoxide | Metabolite | hmdb:HMDB0006558 | |
Aflatoxin M1 | Metabolite | pubchem.compound:15558498 | |
Aflatoxin Q1 | Metabolite | pubchem.compound:104757 | |
AKR7A2 | GeneProduct | ensembl:ENSG00000053371 | |
CYP1A2 | GeneProduct | ensembl:ENSG00000140505 | |
AKR7A3 | GeneProduct | ensembl:ENSG00000162482 | |
GSTT1 | GeneProduct | ensembl:ENSG00000277656 | |
GSTM1 | GeneProduct | ensembl:ENSG00000134184 | |
CYP2A13 | GeneProduct | ensembl:ENSG00000197838 | |
EPHX1 | GeneProduct | ensembl:ENSG00000143819 | |
CYP3A4 | GeneProduct | ensembl:ENSG00000160868 |
References
- Glutathione S-transferase-catalyzed conjugation of bioactivated aflatoxin B(1) in human lung: differential cellular distribution and lack of significance of the GSTM1 genetic polymorphism. Stewart RK, Smith GB, Donnelly PJ, Reid KR, Petsikas D, Conlan AA, et al. Carcinogenesis. 1999 Oct;20(10):1971–7. PubMed Europe PMC Scholia
- Reduction of aflatoxin B1 dialdehyde by rat and human aldo-keto reductases. Guengerich FP, Cai H, McMahon M, Hayes JD, Sutter TR, Groopman JD, et al. Chem Res Toxicol. 2001 Jun;14(6):727–37. PubMed Europe PMC Scholia
- Role of genetic polymorphism of glutathione-S-transferase T1 and microsomal epoxide hydrolase in aflatoxin-associated hepatocellular carcinoma. Tiemersma EW, Omer RE, Bunschoten A, van’t Veer P, Kok FJ, Idris MO, et al. Cancer Epidemiol Biomarkers Prev. 2001 Jul;10(7):785–91. PubMed Europe PMC Scholia
- Reaction of aflatoxin B(1) oxidation products with lysine. Guengerich FP, Arneson KO, Williams KM, Deng Z, Harris TM. Chem Res Toxicol. 2002 Jun;15(6):780–92. PubMed Europe PMC Scholia
- Translational strategies for cancer prevention in liver. Kensler TW, Qian GS, Chen JG, Groopman JD. Nat Rev Cancer. 2003 May;3(5):321–9. PubMed Europe PMC Scholia
- Efficient activation of aflatoxin B1 by cytochrome P450 2A13, an enzyme predominantly expressed in human respiratory tract. He XY, Tang L, Wang SL, Cai QS, Wang JS, Hong JY. Int J Cancer. 2006 Jun 1;118(11):2665–71. PubMed Europe PMC Scholia
- Cytochrome P450s and other enzymes in drug metabolism and toxicity. Guengerich FP. AAPS J. 2006 Mar 10;8(1):E101-11. PubMed Europe PMC Scholia
- CYP2A13 in human respiratory tissues and lung cancers: an immunohistochemical study with a new peptide-specific antibody. Zhu LR, Thomas PE, Lu G, Reuhl KR, Yang GY, Wang LD, et al. Drug Metab Dispos. 2006 Oct;34(10):1672–6. PubMed Europe PMC Scholia
- Aldo-keto reductases and bioactivation/detoxication. Jin Y, Penning TM. Annu Rev Pharmacol Toxicol. 2007;47:263–92. PubMed Europe PMC Scholia
- The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Barski OA, Tipparaju SM, Bhatnagar A. Drug Metab Rev. 2008;40(4):553–624. PubMed Europe PMC Scholia