Protein engineerig of dihydrofolate reductase. pH dependency of Phe-31 mutants.

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概要

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• Site-specific mutations on dihydrofolate reductase from <I>Escherichia coli</I> at the Phe-31 site have generated (Try-31)-DHFR and (Val-31)-DHFR mutant enzymes. The pH dependence of log<I>V</I> and log<I>V</I>⁄<I>K</I><SUB>DHF</SUB> for these enzymes suggests that protonation is important for both the interaction of dihydrofolate and the maximum velocity of the reaction. More importantly, a "hollow" is observed for the Tyr-31 mutant in a log<I>V</I>⁄<I>K</I>–pH profile, necessitating a modification of the wild-type kinetic scheme. The intrinsic p<I>K</I><SUB>a</SUB> of 5.8, obtained based on the modified more general kinetic scheme, for the Tyr-31 mutant agrees well with that obtained from inhibition studies by 2,4-diamino-6,7-dimethylpteridine.

• 公益社団法人 日本化学会の論文

著者

• Chen Jin-Tann

  Development Center for Biotechnology

• Taira Kazunari

  Fermentation Research Institute, Agency of Industrial Science and Technology

• Benkovic Stephen

  Department of Chemistry, The Pennsylvania State University

• Fierke Carol

  Department of Chemistry, The Pennsylvania State University

関連論文

• Protein engineerig of dihydrofolate reductase. pH dependency of Phe-31 mutants.
• Protein engineering of dihydrofolate reductase. Improved catalytic step of mutant-enzymes.

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