ELECTROSTATIC INTERACTION BETWEEN 2 DOMAINS OF ISOCITRATE DEHYDROGENASE FROM THERMUS-THERMOPHILUS IS IMPORTANT FOR THE CATALYTIC FUNCTION AND PROTEIN STABILITY

Authors
YAOI T HAYASHIIWASAKI Y OSHIMA T
Citation
T. Yaoi et al., ELECTROSTATIC INTERACTION BETWEEN 2 DOMAINS OF ISOCITRATE DEHYDROGENASE FROM THERMUS-THERMOPHILUS IS IMPORTANT FOR THE CATALYTIC FUNCTION AND PROTEIN STABILITY, FEBS letters, 398(2-3), 1996, pp. 228-230
Citations number
17
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
398
Issue
2-3
Year of publication
1996
Pages
228 - 230
Database
ISI
SICI code
0014-5793(1996)398:2-3<228:EIB2DO>2.0.ZU;2-4
Abstract
The role of electrostatic interaction between Lys(96) and Glu(147) of isocitrate dehydrogenase from Thermus thermophilus was investigated by site-directed mutagenesis. These two residues are located near the ac tive site and involved in the interdomain interaction. Analyses of the catalytic properties and thermostability of the Glu(147)Gln mutant re vealed that this interaction plays important roles in catalytic functi on and protein stability.