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 journalArticle

14 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 Ala 172 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

Fingerprint

3-Isopropylmalate Dehydrogenase
Thermus thermophilus
Thermodynamic stability
Hot Temperature
Enzymes
Mutagenesis
Molecular modeling
Viperidae
Site-Directed Mutagenesis
Coulomb interactions
Static Electricity
Amino Acids

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus. / Akanuma, Satoshi; Qu, Chunxu; Yamagishi, Akihiko; Tanaka, Nobuo; Oshima, Tairo.

In: FEBS Letters, Vol. 410, No. 2-3, 30.06.1997, p. 141-144.

Research output: Contribution to journalArticle

Akanuma, Satoshi ; Qu, Chunxu ; Yamagishi, Akihiko ; Tanaka, Nobuo ; Oshima, Tairo. / Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus. In: FEBS Letters. 1997 ; Vol. 410, No. 2-3. pp. 141-144.
@article{9053b09beefb49c4ba66be559d7660fa,
title = "Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus",
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 Ala 172 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.",
keywords = "3-Isopropylmalate dehydrogenase, Electrostatic interaction, Hydrophobic packing, Site-directed mutagenesis, Thermal stability",
author = "Satoshi Akanuma and Chunxu Qu and Akihiko Yamagishi and Nobuo Tanaka and Tairo Oshima",
year = "1997",
month = "6",
day = "30",
doi = "10.1016/S0014-5793(97)00540-1",
language = "English",
volume = "410",
pages = "141--144",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2-3",

}

TY - JOUR

T1 - Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus

AU - Akanuma, Satoshi

AU - Qu, Chunxu

AU - Yamagishi, Akihiko

AU - Tanaka, Nobuo

AU - Oshima, Tairo

PY - 1997/6/30

Y1 - 1997/6/30

N2 - 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 Ala 172 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.

AB - 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 Ala 172 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.

KW - 3-Isopropylmalate dehydrogenase

KW - Electrostatic interaction

KW - Hydrophobic packing

KW - Site-directed mutagenesis

KW - Thermal stability

UR - http://www.scopus.com/inward/record.url?scp=0030785695&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030785695&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(97)00540-1

DO - 10.1016/S0014-5793(97)00540-1

M3 - Article

C2 - 9237617

AN - SCOPUS:0030785695

VL - 410

SP - 141

EP - 144

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2-3

ER -