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Substrate specificity of mutated cytochrome P450 (CYP102A5) from Bacillus cereus ATCC14579

원문정보

Changhyun Roh, Hyung-Yeon Park, Kwon-Young Choi, Bishnu Prasad Pandey, June-Hyung Kim, Byung-Gee Kim

한국생물공학회 한국생물공학회 학술대회 2007 춘계학술대회 및 국제심포지움 2007.04 pp.25-25
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초록

영어

Cytochrome P450s act on the inactive carbon-hydrogen bonds of alkanes, fatty acids, terpenes, and steroids [1]. And some exhibits high regio and stereoselective monooxygenation activity. The CYP102A5 is a 120 kDa (1065 aa) self-sufficient monooxygenase which belongs to Class III, consisting of an FMN/FAD-containing reductase domain and a heme domain. The gene encoding CYP102A5, a novel P450 monooxygenase from Bacillus cereus, was cloned and expressed in Escherichia coliBL21 using pET expression system. The CYP102A5 of wild type catalyses the oxidation of alkanes, alkanoic acids and unsaturated fatty acids. Furthermore,
double mutant F90V T441G L442G exhibited its activity towards daidzein of biphenolic compound. Furthermore, this triple mutant catalyzed regioselective hydroxylation at the 6, 8 and 3' position of daidzein.

저자정보

  • Changhyun Roh School of Chemical and Biological Engineering, Seoul National University, Institute of Molecular Biology and Genetics
  • Hyung-Yeon Park Department of Chemistry, Inha University
  • Kwon-Young Choi School of Chemical and Biological Engineering, Seoul National University, Institute of Molecular Biology and Genetics
  • Bishnu Prasad Pandey School of Chemical and Biological Engineering, Seoul National University, Institute of Molecular Biology and Genetics
  • June-Hyung Kim Department of Chemical Engineering, Dong-A University
  • Byung-Gee Kim School of Chemical and Biological Engineering, Seoul National University, Institute of Molecular Biology and Genetics

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