Article
A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.
European journal of biochemistry - 15 Aug 1994
Goward C R, Miller J, Nicholls D J, Irons L I, Scawen M D, O'Brien R, Chowdhry B Z
Abstract excerpt
The stability of wild-type Escherichia coli malate dehydrogenase was compared with a mutant form of the enzyme with the amino acid residue at position 102 changed from arginine to glutamine. The mutation occurs on the underside of a mobile loop which closes over the active-site cleft on formation...
Topics
- Arginine
- Base Sequence
- Calorimetry, Differential Scanning
- Circular Dichroism
- Escherichia coli
- Glutamine
- Malate Dehydrogenase
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Substrate Specificity
- Temperature