Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.

@article{Chen2012CrystalSO,
  title={Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.},
  author={Chung-De Chen and Chih-Hao Lin and Phimonphan Chuankhayan and Y Huang and Y Hsieh and Tien-Feng Huang and Hong-Hsiang Guan and Ming-yih Liu and Wen-Chang Chang and Chun-Jung Chen},
  journal={Journal of bacteriology},
  year={2012},
  volume={194 22},
  pages={6206-16}
}
Branched-chain aminotransferases (BCAT), which utilize pyridoxal 5'-phosphate (PLP) as a cofactor, reversibly catalyze the transfer of the α-amino groups of three of the most hydrophobic branched-chain amino acids (BCAA), leucine, isoleucine, and valine, to α-ketoglutarate to form the respective branched-chain α-keto acids and glutamate. The BCAT from Deinococcus radiodurans (DrBCAT), an extremophile, was cloned and expressed in Escherichia coli for structure and functional studies. The crystal… CONTINUE READING
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