Substrate Recognition Mechanism of Thermophilic Dual-Substrate Enzyme.

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概要

• 論文の詳細を見る

• Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292 residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.

• 社団法人 日本生化学会の論文

著者

• NAKAI Tadashi

  Department of Chemistry, Graduate School of Science, Osaka City University

• Nakai Tadashi

  Department Of Chemistry Graduate School Of Science Osaka City University

• Kuramitsu Seiki

  Department Of Bioligy Graduate School Of Science Osaka University

• Hirotsu Ken

  Department Of Chemistry Faculty Of Science Osaka City University

• Miyahara Ikuko

  Department Of Chemistry Faculty Of Science Osaka City University

• Ura Hideaki

  Department Of Biology Graduate School Of Science Osaka University

• Kawaguchi Shin-ichi

  Department Of Biology Graduate School Of Science Osaka University

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