Article
Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.
The Biochemical journal - 15 Jan 1995
Alldread R M, Halsall D M, Clarke A R, Sundaram T K, Atkinson T, Scawen M D, Nicholls D J
Abstract excerpt
The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the cofactor. This residue is highly conserved as aspartate in malate dehydrogenases, except in the t...
Topics
- Aspartic Acid
- Base Sequence
- Catalysis
- Enzyme Stability
- Glutamic Acid
- Hot Temperature
- Malate Dehydrogenase
- Models, Chemical
- Molecular Sequence Data
- Mutagenesis
- Mutation
- NAD
- Oxaloacetates
- Oxidation-Reduction
- Protein Conformation
- Recombinant Proteins
- Solvents
- Structure-Activity Relationship