Crystal structure analysis of .OMEGA.-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation.
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概要
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The three-dimensional structure of ω-amino acid:pyruvate aminotransferase from Pseudomonas sp. F-126, an isologous α4 tetramer containing pyridoxal 5'-phosphate (PLP) as a cofactor, has been determined at 2.0 A resolution. The diffraction data were collected with a newly developed Weissenberg camera with a Fuji Imaging Plate, using synchrotron radiation. The mean figure-of-merit was 0.57. The subunit is rich in secondary structure and comprises two domains. PLP is located in the large domain. The high homology in the secondary structure between this enzyme and aspartate aminotransferase strongly indicates that these two types of enzymes have evolved from a common ancestor.
- 社団法人 日本生化学会の論文
著者
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Aibara Shigeo
The Research Institute For Food Science Kyoto University
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Morita Yuhei
The Research Institute For Food Science Kyoto University
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Fukutani Hirohito
Institute Of Physics College Of General Education University Of Tokyo
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Yonaha Kazuo
Department Of Agricultural Chemistry University Of Ryukyus
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Sakabe Kiwako
Department Of Chemistry Faculty Of Science Nagoya University
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Sasaki Kyoyu
College Of Medical Technology Nagoya University
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TOYAMA Seizen
Department of Agricultural Chemistry, University of the Ryukyus
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Watanabe Nobuhisa
Institute of Physics, University of Tsukuba
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Sakabe Noriyoshi
Photon Factory, National Laboratory for High Energy Physics
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Higashi Tsuneyuki
Department of Pharmaceutical Science, Kyoto University
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