Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method

Takashi Kotsuka, Satoshi Akanuma, Masaaki Tomuro, Akihiko Yamagishi, Tairo Oshima*

*この研究の対応する著者

研究成果: Article査読

60 被引用数 (Scopus)

抄録

We succeeded in further improvement of the stability of 3-isopropylmalate dehydrogenase (IPMDH) from an extreme thermophile, Thermus thermophilus, by a suppressor mutation method. We previously constructed a chimeric IPMDH consisting of portions of thermophile and mesophile enzymes. The chimeric enzyme is less thermostable than the thermophile enzyme. The gene encoding the chimeric enzyme was subjected to random mutagenesis and integrated into the genome of a leuB-deficient mutant of T. thermophilus. The transformants were screened at 76°C in minimum medium, and three independent stabilized mutants were obtained. The leuB genes from these three mutants were cloned and analyzed. The sequence analyses revealed Ala-172→Val substitution in all of the mutants. The thermal stability of the thermophile IPMDH was improved by introducing the amino acid substitution.

本文言語English
ページ(範囲)723-727
ページ数5
ジャーナルJournal of Bacteriology
178
3
DOI
出版ステータスPublished - 1996 2月
外部発表はい

ASJC Scopus subject areas

  • 微生物学
  • 分子生物学

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