Properties and function of malate enzyme from Pseudomonas putida.

@article{GarridoPertierra1983PropertiesAF,
  title={Properties and function of malate enzyme from Pseudomonas putida.},
  author={Amando Garrido-Pertierra and C Martinez Marcos and M Martin Fernandez and M. Ruiz-Amil},
  journal={Biochimie},
  year={1983},
  volume={65 11-12},
  pages={629-35}
}
Malate enzyme (L-malate: NADP+ oxidoreductase (oxalacetate-decarboxylating, EC 1.1.1.40)) has been purified from Pseudomonas putida to 99 per cent homogeneity by heat, ammonium suphate fractionation, gel filtration and anion exchange chromatography. Sodium dodecylsulphate-(SDS)-polyacrylamide disc gel electrophoresis analysis showed an approximate tetrameric subunit with a molecular weight of 52,000. The purified enzyme showed a pH optimum between 8.0 and 8.5 (for Tris-HCl buffer) and required… CONTINUE READING