Citation
Uno, Yasuhiro, et al. "2-Oxidation, 3-methyl Hydroxylation, and 6-hydroxylation of Skatole, a Contributor to the Odour of Boar-tainted Pork Meat, Mediated By Porcine Liver Microsomal Cytochromes P450 1A2, 2A19, 2E1, and 3A22." Xenobiotica; the Fate of Foreign Compounds in Biological Systems, 2023, pp. 1-6.
Uno Y, Morikuni S, Murayama N, et al. 2-Oxidation, 3-methyl hydroxylation, and 6-hydroxylation of skatole, a contributor to the odour of boar-tainted pork meat, mediated by porcine liver microsomal cytochromes P450 1A2, 2A19, 2E1, and 3A22. Xenobiotica. 2023.
Uno, Y., Morikuni, S., Murayama, N., & Yamazaki, H. (2023). 2-Oxidation, 3-methyl hydroxylation, and 6-hydroxylation of skatole, a contributor to the odour of boar-tainted pork meat, mediated by porcine liver microsomal cytochromes P450 1A2, 2A19, 2E1, and 3A22. Xenobiotica; the Fate of Foreign Compounds in Biological Systems, 1-6. https://doi.org/10.1080/00498254.2023.2197037
Uno Y, et al. 2-Oxidation, 3-methyl Hydroxylation, and 6-hydroxylation of Skatole, a Contributor to the Odour of Boar-tainted Pork Meat, Mediated By Porcine Liver Microsomal Cytochromes P450 1A2, 2A19, 2E1, and 3A22. Xenobiotica. 2023 Apr 5;1-6. PubMed PMID: 36976910.
TY - JOUR
T1 - 2-Oxidation, 3-methyl hydroxylation, and 6-hydroxylation of skatole, a contributor to the odour of boar-tainted pork meat, mediated by porcine liver microsomal cytochromes P450 1A2, 2A19, 2E1, and 3A22.
AU - Uno,Yasuhiro,
AU - Morikuni,Saho,
AU - Murayama,Norie,
AU - Yamazaki,Hiroshi,
Y1 - 2023/04/05/
PY - 2023/3/29/pubmed
PY - 2023/3/29/medline
PY - 2023/3/28/entrez
KW - 3-methyloxindole
KW - 6-hydroxyskatole
KW - Boar taint
KW - indole-3-carbinol
KW - pig
KW - sex differences
SP - 1
EP - 6
JF - Xenobiotica; the fate of foreign compounds in biological systems
JO - Xenobiotica
N2 - 1. The 2-oxidation, 3-methyl hydroxylation, and 6-hydroxylation of skatole (a contributor to boar taint) mediated by minipig liver microsomes and recombinant P450 enzymes expressed in bacterial membranes were investigated.2. At low substrate concentrations of 10 µM, the formation rates of indole-3-carbinol, 6-hydroxyskatole, and the sum of 3-methyloxindole, indole-3-carbinol, and 6-hydroxyskatole in male minipig liver microsomes were significantly lower than those in female minipig liver microsomes.3. Compensatory 3-methyloxindole and indole-3-carbinol formation in minipig liver microsomes, which lack 6-hydroxyskatole formation in males, was mediated partly by liver microsomal P450 1A2 and P450 1A2/2E1, respectively. These enzymes were suppressed by typical P450 inhibitors in female minipig liver microsomes.4. Among the 14 pig P450 forms evaluated, P450 2A19 was the dominant form mediating 3-methyloxindole, indole-3-carbinol, and 6-hydroxyskatole formation from skatole at substrate concentrations of 100 µM. Positive cooperativity was observed in 3-methyloxindole formation from skatole mediated by male minipig liver microsomes and by pig P450 3A22 with Hill coefficients of 1.2-1.5.5. These results suggest high skatole 2-oxidation, 3-methyl hydroxylation, and 6-hydroxylation activities of pig P450 2A19 and compensatory skatole oxidations mediated by pig P450 1A2, 2E1, or 3A22 in male minipig liver microsomes.
SN - 1366-5928
UR - https://www.unboundmedicine.com/medline/citation/36976910/2_Oxidation_3_methyl_hydroxylation_and_6_hydroxylation_of_skatole_a_contributor_to_the_odour_of_boar_tainted_pork_meat_mediated_by_porcine_liver_microsomal_cytochromes_P450_1A2_2A19_2E1_and_3A22_
DB - PRIME
DP - Unbound Medicine
ER -
