Crystal Structure of Prolyl Aminopeptidase from Serratia marcescens.
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概要
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Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 Å resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the α/β hydrolase fold, with a central eight-stranded β-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.
- 社団法人 日本生化学会の論文
著者
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Kabashima Tsutomu
School Of Pharmaceutical Sciences Nagasaki University
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Tsuru Masato
Information Science Center Nagasaki University
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Ito Kiyoshi
School Of Pharmaceutical Sciences Nagasaki University
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INOUE Takahiko
School of Pharmaceutical Sciences, Nagasaki University
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TANAKA Nobutada
School of Pharmaceutical Sciences, Showa University
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Nakamura Kazuo
School Of Pharmaceutical Science Showa University
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Uchikawa Kouichirou
School of Pharmaceutical Sciences, Nagasaki University
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Yoshimoto Tadashi
School of Pharamaceutical Sciences, Nagasaki University
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