Identification of Amino Acid Residues Essential for the Catalytic Reaction of Bacillus kaustophilus Leucine Aminopeptidase
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概要
- 論文の詳細を見る
The functional significance of amino acid residues Lys-265, Asp-270, Lys-277, Asp-288, Asp-347, Glu-349, and Arg-351 of Bacillus kaustophilus leucine aminopeptidase was explored by site-directed mutagenesis. Variants with an apparent molecular mass of approximately 54 kDa were overexpressed in Escherichia coli and purified to homogeneity by nickel-chelate chromatography. The purified mutant enzymes had no LAP activity, implying that these residues are important for the catalytic reaction of the enzyme.
- 社団法人 日本農芸化学会の論文
- 2004-08-23
著者
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Lin Long-Liu
Department of Applied Chemistry, National Chiayi University
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Lin L‐l
Department Of Applied Chemistry National Chiayi University
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Chi M‐c
Graduate Institute Of Biotechnology National Chiayi University
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Chi Meng-chun
Graduate Institute Of Biotechnology National Chiayi University
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CHOU Wei-Mou
Graduate Institute of Biotechnology, National Chiayi University
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HSU Wen-Hwei
Institute of Molecular Biology, National Chung Hsing University
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Hsu Wen-hwei
Institute Of Molecular Biology National Chung Hsing University
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Chou Wei-mou
Graduate Institute Of Biotechnology National Chiayi University
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Lin Long-liu
Department Of Applied Chemistry National Chia-yi University
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