Article
A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
Biochemistry - 12 Aug 1997
Schliebs W, Thanki N, Jaenicke R, Wierenga R K
Abstract excerpt
Triosephosphate isomerase (TIM) is a very stable dimer. In order to understand better the importance of dimerization for stability and catalytic activity, we have constructed a monomeric double-mutation variant. The dimer interface residues Thr75 and Gly76, which are at the tip of loop 3, have be...
Topics
- Catalysis
- Dimerization
- Enzyme Activation
- Enzyme Stability
- Genetic Variation
- Kinetics
- Mutagenesis, Site-Directed
- Thermodynamics
- Triose-Phosphate Isomerase