| 학회 |
한국공업화학회 |
| 학술대회 |
2009년 봄 (04/15 ~ 04/17, 호텔인터불고(대구)) |
| 권호 |
13권 1호 |
| 발표분야 |
생물공학 |
| 제목 |
Protein Engineering of CYP102A1 and CYP102A7 for the hydroxylation of Polycyclic Aromatic Hydrocarbons |
| 초록 |
Cytochrome P450s are ubiquitously distributed enzymes that are present in plants, bacteria, and mammals. These heme-thiolate proteins have unique catalystic activities as oxidants and monooxygenases towards their substrates.CYP102A1(P450 BM3) from Bacillus megaterium, which records highest turnover rate and activity for a P450,and CYP102A7(Bacillus licheniformis). Site specific mutagenesis and directed evolution have been employed to improve their limited activities towards polycyclic aromatic hydrocarbons(PAH) and flavonoids which show anti-oxidant acitivity. CYP102A1 and CYP102A7, P450 from were each specifically engineered to change the substrate specificity and to increase the minor catalytic activity. |
| 저자 |
고성기, 최권영, 김태진, 이나훔, 비쉬누 판데이, 김병기
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| 소속 |
서울대 |
| 키워드 |
cytochrome; P450; site-directed mutagenesis; BM-3
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| E-Mail |
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