A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.

@article{Goward1994ASA,
  title={A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.},
  author={C R Goward and Jean Miller and David J. Nicholls and L. I. Irons and Michael D. Scawen and Ronan O'Brien and Babur Z. Chowdhry},
  journal={European journal of biochemistry},
  year={1994},
  volume={224 1},
  pages={249-55}
}
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 of the enzyme/cofactor/substrate ternary complex. The mutant enzyme is kinetically compromised while the wild-type enzyme is highly specific for oxaloacetate. The mutant enzyme was shown to be more… CONTINUE READING