Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.

@article{Jhee2000StereochemistryOT,
  title={Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.},
  author={Kwang Hwan Jhee and Toshiaki Yoshimura and Edith Wilson Miles and Shigeki Takeda and Ikuko Miyahara and Ken Hirotsu and Kenji Soda and Yuuki Kawata and Nobuyoshi Esaki},
  journal={Journal of biochemistry},
  year={2000},
  volume={128 4},
  pages={
          679-86
        }
}
Aminodeoxychorismate lyase is a pyridoxal 5'-phosphate-dependent enzyme that converts 4-aminodeoxychorismate to pyruvate and p-aminobenzoate, a precursor of folic acid in bacteria. The enzyme exhibits significant sequence similarity to two aminotransferases, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase. In the present study, we have found that aminodeoxychorismate lyase catalyzes the transamination between D-alanine and pyridoxal phosphate to produce pyruvate… CONTINUE READING