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포스터 발표 : 효소공학

Evolution of CYP102D1 from Streptomyces avermitilis to Increase Hydroxylation Activity towards Kaempferol

원문정보

Byeo-Ri AN, Kwon-young CHOI, Eunok JUNG, Da-Hye JUNG, Wonji CHOI, Byung-Gee KIM

한국생물공학회 한국생물공학회 학술대회 2012 춘계학술대회 및 국제심포지움 2012.04 pp.177-177
피인용수 : 0건 (자료제공 : 네이버학술정보)

초록

영어

Flavonols possess antioxidant and free radical scavenging activity in foods, with myricetin being one of the most active. In plant, kaempferol converts to myricetin by 3’, 5’-hydroxylase which is cytochrome P450. The cytochrome P450s belong to a family of heme containing monooxygenases and catalyze diverse reaction, such as hydroxylation, epoxidation and O-demethylation. CYP102D1, bi-functional cytochrome P450:NADPH-P450 reductase, from Streptomyces avermitilis can hydroxylate the saturated and unsaturated fatty acids. First, three positions, which are L84A/F96V/L448A, were done saturation mutagenesis to increase the size of active site pocket and substrate access channel. Second, A273/G274/T277 was selected among the amino acid within 7Å from heme to saturated mutagenesis. For high throughput screening, aldehyde sensing method was applied with schiff’s test. Finally, we screened six CYP102 mutants towards permethylated kaempferol using schiff’s reagent agar plate assay and expressed.

키워드

저자정보

  • Byeo-Ri AN Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.
  • Kwon-young CHOI Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.
  • Eunok JUNG Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.
  • Da-Hye JUNG Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.
  • Wonji CHOI Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.
  • Byung-Gee KIM Dept. of Chemical and Biological Engineering, Seoul National University, Seoul, Korea.

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자료제공 : 네이버학술정보

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