Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 2003.06a
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- Pages.70-70
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- 2003
The active site and substrate binding mode of 1-aminocyclopropane-1- carboxylate oxidase of Fuji apple (Malus domesticus L.) determined by site directed mutagenesis and comparative modeling studies
- Ahrim Yoo (Department of Chemical and Biological Engineering, Korea University) ;
- Seo, Young-Sam (Department of Biology, College of Science, Yonsei University) ;
- Sung, Soon-Kee (Plant Biotechnology Team, Dongbu Advanced Research Institute) ;
- Yang, Dae-Ryook (Department of Chemical and Biological Engineering, Korea University) ;
- Kim, Woo-Tae-K (Department of Biology, College of Science, Yonsei University) ;
- Lee, Weontae (Department of Biochemistry, College of Science, Yonsei University)
- Published : 2003.06.01
Abstract
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
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