Characterization of amino acid aminotransferases of Methanococcus aeolicus.

@article{Xing1992CharacterizationOA,
  title={Characterization of amino acid aminotransferases of Methanococcus aeolicus.},
  author={Ruihuan Xing and William B. Whitman},
  journal={Journal of bacteriology},
  year={1992},
  volume={174 2},
  pages={541-8}
}
Four aminotransferases were identified and characterized from Methanococcus aeolicus. Branched-chain aminotransferase (BcAT, EC 2.6.1.42), aspartate aminotransferase (AspAT, EC 2.6.1.1), and two aromatic aminotransferases (EC 2.6.1.57) were partially purified 175-, 84-, 600-, and 30-fold, respectively. The apparent molecular weight, substrate specificity, and kinetic properties of the BcAT were similar to those of other microbial BcATs. The AspAT had an apparent molecular weight of 162,000… CONTINUE READING