Highly Conservative Sequence in the Carboxyl Terminus of Sarcosine Oxidase is Important for Substrate Binding
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概要
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The function of the highly conservative sequence -G(344)-F-S-G-H-G-F-K-F(352)-in the carboxyl terminus of sarcosine oxidase was investigated using site-directed mutagenesis. When H-348 was substituted with uncharged amino acids, the K_m values of sarcosine oxidase markedly increased, although the k_<cat> values remained the same as that of the wild-type enzyme. The kinetic parameters obtained with other mutations also suggested that the conservative sequence acts as the substrate-binding site. When K-351 was replaced by Ala, the mutant K351A could not bind the coenzyme FAD (flavin adenine dinucleotide). This result suggested that K-351 interacts with the FAD-binding site of the amino-terminal region. The enzymic activities of the mutants H348Q and H348A were lost at neutral and acidic pH as a result of the disappearance of the positive charge on H-348.
- 公益社団法人日本生物工学会の論文
- 1997-12-25
著者
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Nishiya Yoshiaki
Tsuruga Institute Of Biotechnology Toyobo Co. Ltd.
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Imanaka Tadayuki
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering Kyoto Univ
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