Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum

@article{Yennaco2007CharacterizationOM,
  title={Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum},
  author={Lynda J. Yennaco and Yajing Hu and James F Holden},
  journal={Extremophiles},
  year={2007},
  volume={11},
  pages={741-746}
}
Native and recombinant malate dehydrogenase (MDH) was characterized from the hyperthermophilic, facultatively autotrophic archaeon Pyrobaculum islandicum. The enzyme is a homotetramer with a subunit mass of 33 kDa. The activity kinetics of the native and recombinant proteins are the same. The apparent K m values of the recombinant protein for oxaloacetate (OAA) and NADH (at 80°C and pH 8.0) were 15 and 86 μM, respectively, with specific activity as high as 470 U mg−1. Activity decreased more… CONTINUE READING