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

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)141-144
Number of pages4
JournalFEBS Letters
Volume410
Issue number2-3
DOIs
Publication statusPublished - 1997 Jun 30
Externally publishedYes

Keywords

  • 3-Isopropylmalate dehydrogenase
  • Electrostatic interaction
  • Hydrophobic packing
  • Site-directed mutagenesis
  • Thermal stability

ASJC Scopus subject areas

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

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