Amino Acid Substitutions in the Subunit Interface Enhancing Thermostability ofThermoplasma acidophilumCitrate Synthase
- 19 August 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 249 (2) , 566-571
- https://doi.org/10.1006/bbrc.1998.9192
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- The Crystal Structure of Citrate Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus at 1.9 Å Resolution,Biochemistry, 1997
- Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation methodJournal of Bacteriology, 1996
- Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosusProtein Engineering, Design and Selection, 1995
- The crystal structure of citrate synthase from the thermophilic Archaeon, Thermoplasma acidophilumStructure, 1994
- A Very Short Hydrogen Bond Provides Only Moderate Stabilization of an Enzyme-Inhibitor Complex of Citrate SynthaseBiochemistry, 1994
- Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilusEuropean Journal of Biochemistry, 1994
- Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolutionJournal of Molecular Biology, 1991
- Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilumEuropean Journal of Biochemistry, 1990
- Crystallographic refinement and atomic models of two different forms of citrate synthase at 2·7 and 1·7 Å resolutionJournal of Molecular Biology, 1982
- Complete amino acid sequence of porcine heart citrate synthaseBiochemistry, 1982