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

*この研究の対応する著者

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月 30
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

フィンガープリント

「Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル