| 학회 |
한국화학공학회 |
| 학술대회 |
2003년 가을 (10/24 ~ 10/25, 한양대학교) |
| 권호 |
9권 2호, p.2149 |
| 발표분야 |
생물화공 |
| 제목 |
The active site and substrate binding mode of 1-aminocyclopropane-1-carboxylate oxidase of apple (Malus domestica Borkh. cv. Golden delicious) fruit determined by site-directed mutagenesis and comparative modeling studies |
| 초록 |
Active sites and substrate bindings of 1-aminoxyclopropane-1-carboxylate oxidase (MD-ACO1) catalyzing the oxidative conversion of ACC to ethylene have been determined based on site-directed mutagenesis and comparative modeling methods. Molecular modeling based on the crystal structure of Isopenicillin N synthase (IPNS) provided MD-ACO1 structure. MD-ACO1 protein folds into a compact jelly roll shape, consisting of 9 α-helices, 10 β-strands and several long loops. The MD-ACO1/ACC/Fe(II)/Ascorbate complex conformation was determined from automated docking program, AUTODOCK. The MD-ACO1/FeII complex model was consistent with well known binding motif information (HIS177-ASP179-HIS234). The cosubstrate, ascorbate is placed between iron binding pocket and Arg244 of MD-ACO1 enzyme, supporting the critical role of Arg244 for generating reaction product. These findings are strongly supported by previous biochemical data as well as site-directed mutagenesis data. |
| 저자 |
유아림1, 서영삼2, 성순기3, 김우택2, 이원태2, 양대륙1
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| 소속 |
1고려대, 2연세대, 3동부(연) |
| 키워드 |
ethylene;Comparative modeling;MD-ACO1;Modeller |
| E-Mail |
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| 원문파일 |
초록 보기 |
