Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus

Satoshi Akanuma, Chunxu Qu, Akihiko Yamagishi, Nobuo Tanaka, Tairo Oshima

研究成果: Article査読

15 被引用数 (Scopus)

抄録

To understand the role of the amino acid residue at position 172 in the conformational stability, four mutant enzymes of Thermus thermophilus 3- isopropylmalate dehydrogenase in which Ala172 was replaced with Asp, Glu, Asn, and Gln were prepared by site-directed mutagenesis. Three mutants were more stable than the wild-type enzyme. No significant change in catalytic properties was found in the mutant enzymes. The molecular modeling studies suggested that the enhanced thermostability of the mutant enzymes resulted from the formation of extra electrostatic interactions and/or improvement of hydrophobic packing of the interior core.

本文言語English
ページ(範囲)141-144
ページ数4
ジャーナルFEBS Letters
410
2-3
DOI
出版ステータスPublished - 1997 6 30
外部発表はい

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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