Oxidation of 1-chloropyrene by human CYP1 family and CYP2A subfamily cytochrome P450 enzymes: catalytic roles of two CYP1B1 and five CYP2A13 allelic variants
1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4 and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CY...
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| Published in | Xenobiotica Vol. 48; no. 6; pp. 565 - 575 |
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| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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England
03.06.2018
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| Abstract | 1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4 and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CYP1B1 and five CYP2A13 allelic variants were also examined. 2. CYP1A1 oxidized 1-chloropyrene at the 6- and 8-positions more actively than at the 3-position, while both CYP1B1.1 and 1B1.3 preferentially catalyzed 6-hydroxylation. 3. Five CYP2A13 allelic variants oxidized 8-hydroxylation much more than 6- and 3-hydroxylation, and the variant CYP2A13.3 was found to slowly catalyze these reactions with a lower k
value than other CYP2A13.1 variants. 4. CYP2A6 catalyzed 1-chloropyrene 6-hydroxylation at a higher rate than the CYP2A13 enzymes, but the rate was lower than the CYP1A1 and 1B1 variants. Other human P450 enzymes had low activities towards 1-chloropyrene. 5. Molecular docking analysis suggested differences in the interaction of 1-chloropyrene with active sites of CYP1 and 2 A enzymes. In addition, a naturally occurring Thr134 insertion in CYP2A13.3 was found to affect the orientation of Asn297 in the I-helix in interacting with 1-chloropyrene (and also 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, NNK) and caused changes in the active site of CYP2A13.3 as compared with CYP2A13.1. |
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| AbstractList | 1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4 and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CYP1B1 and five CYP2A13 allelic variants were also examined. 2. CYP1A1 oxidized 1-chloropyrene at the 6- and 8-positions more actively than at the 3-position, while both CYP1B1.1 and 1B1.3 preferentially catalyzed 6-hydroxylation. 3. Five CYP2A13 allelic variants oxidized 8-hydroxylation much more than 6- and 3-hydroxylation, and the variant CYP2A13.3 was found to slowly catalyze these reactions with a lower kcat value than other CYP2A13.1 variants. 4. CYP2A6 catalyzed 1-chloropyrene 6-hydroxylation at a higher rate than the CYP2A13 enzymes, but the rate was lower than the CYP1A1 and 1B1 variants. Other human P450 enzymes had low activities towards 1-chloropyrene. 5. Molecular docking analysis suggested differences in the interaction of 1-chloropyrene with active sites of CYP1 and 2 A enzymes. In addition, a naturally occurring Thr134 insertion in CYP2A13.3 was found to affect the orientation of Asn297 in the I-helix in interacting with 1-chloropyrene (and also 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, NNK) and caused changes in the active site of CYP2A13.3 as compared with CYP2A13.1. Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4, and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CYP1B1 and five CYP2A13 allelic variants were also examined. CYP1A1 oxidized 1-chloropyrene at the 6- and 8-positions more actively than at the 3-position, while both CYP1B1.1 and 1B1.3 preferentially catalyzed 6-hydroxylation. Five CYP2A13 allelic variants oxidized 8-hydroxylation much more than 6- and 3-hydroxylation, and the variant CYP2A13.3 was found to slowly catalyze these reactions with a lower k cat value than other CYP2A13.1 variants. CYP2A6 catalyzed 1-chloropyrene 6-hydroxylation at a higher rate than the CYP2A13 enzymes, but the rate was lower than the CYP1A1 and 1B1 variants. Other human P450 enzymes had low activities towards 1-chloropyrene. Molecular docking analysis suggested differences in the interaction of 1-chloropyrene with active sites of CYP1 and 2A enzymes. In addition, a naturally occuring Thr134 insertion in CYP2A13.3 was found to affect the orientation of Asn297 in the I-helix in interacting with 1-chloropyrene (and also 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, NNK) and caused changes in the active site of CYP2A13.3 as compared with CYP2A13.1. 1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4 and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CYP1B1 and five CYP2A13 allelic variants were also examined. 2. CYP1A1 oxidized 1-chloropyrene at the 6- and 8-positions more actively than at the 3-position, while both CYP1B1.1 and 1B1.3 preferentially catalyzed 6-hydroxylation. 3. Five CYP2A13 allelic variants oxidized 8-hydroxylation much more than 6- and 3-hydroxylation, and the variant CYP2A13.3 was found to slowly catalyze these reactions with a lower k value than other CYP2A13.1 variants. 4. CYP2A6 catalyzed 1-chloropyrene 6-hydroxylation at a higher rate than the CYP2A13 enzymes, but the rate was lower than the CYP1A1 and 1B1 variants. Other human P450 enzymes had low activities towards 1-chloropyrene. 5. Molecular docking analysis suggested differences in the interaction of 1-chloropyrene with active sites of CYP1 and 2 A enzymes. In addition, a naturally occurring Thr134 insertion in CYP2A13.3 was found to affect the orientation of Asn297 in the I-helix in interacting with 1-chloropyrene (and also 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, NNK) and caused changes in the active site of CYP2A13.3 as compared with CYP2A13.1. |
| Author | Shimada, Tsutomu Yamazaki, Hiroshi Murayama, Norie Lim, Young-Ran Yeom, Sora Komori, Masayuki Takenaka, Shigeo Kim, Donghak Kakimoto, Kensaku Guengerich, F Peter |
| AuthorAffiliation | 2 Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Machida, Tokyo 194-8543 6 Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA 4 Graduate School of Comprehensive Rehabilitation, Osaka Prefecture University, 3-7-30, Habikino, Habikino-shi, Osaka 583-8555 5 Department of Biological Sciences, Konkuk University, Seoul 05029, Korea 3 Osaka Institute of Public Health, 1-3-69 Nakamichi, Higashinari-ku, Osaka 537-0025 1 Laboratory of Cellular and Molecular Biology, Osaka Prefecture University, 1-58 Rinku-Orai-Kita, Izumisano, Osaka 598-8531 |
| AuthorAffiliation_xml | – name: 4 Graduate School of Comprehensive Rehabilitation, Osaka Prefecture University, 3-7-30, Habikino, Habikino-shi, Osaka 583-8555 – name: 5 Department of Biological Sciences, Konkuk University, Seoul 05029, Korea – name: 3 Osaka Institute of Public Health, 1-3-69 Nakamichi, Higashinari-ku, Osaka 537-0025 – name: 6 Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA – name: 2 Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Machida, Tokyo 194-8543 – name: 1 Laboratory of Cellular and Molecular Biology, Osaka Prefecture University, 1-58 Rinku-Orai-Kita, Izumisano, Osaka 598-8531 |
| Author_xml | – sequence: 1 givenname: Tsutomu surname: Shimada fullname: Shimada, Tsutomu organization: a Laboratory of Cellular and Molecular Biology, Osaka Prefecture University , Osaka , Japan – sequence: 2 givenname: Norie surname: Murayama fullname: Murayama, Norie organization: b Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University , Machida , Tokyo – sequence: 3 givenname: Kensaku surname: Kakimoto fullname: Kakimoto, Kensaku organization: c Osaka Institute of Public Health , Osaka , Japan – sequence: 4 givenname: Shigeo surname: Takenaka fullname: Takenaka, Shigeo organization: d Graduate School of Comprehensive Rehabilitation, Osaka Prefecture University , Osaka , Japan – sequence: 5 givenname: Young-Ran surname: Lim fullname: Lim, Young-Ran organization: e Department of Biological Sciences , Konkuk University , Seoul , Korea , and – sequence: 6 givenname: Sora surname: Yeom fullname: Yeom, Sora organization: e Department of Biological Sciences , Konkuk University , Seoul , Korea , and – sequence: 7 givenname: Donghak surname: Kim fullname: Kim, Donghak organization: e Department of Biological Sciences , Konkuk University , Seoul , Korea , and – sequence: 8 givenname: Hiroshi surname: Yamazaki fullname: Yamazaki, Hiroshi organization: b Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University , Machida , Tokyo – sequence: 9 givenname: F Peter surname: Guengerich fullname: Guengerich, F Peter organization: f Department of Biochemistry , Vanderbilt University School of Medicine , Nashville, TN , USA – sequence: 10 givenname: Masayuki surname: Komori fullname: Komori, Masayuki organization: a Laboratory of Cellular and Molecular Biology, Osaka Prefecture University , Osaka , Japan |
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| Snippet | 1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes... Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes... |
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| Title | Oxidation of 1-chloropyrene by human CYP1 family and CYP2A subfamily cytochrome P450 enzymes: catalytic roles of two CYP1B1 and five CYP2A13 allelic variants |
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