Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.

@article{Kataoka1997IsolationAC,
  title={Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.},
  author={Michihiko Kataoka and M Ikemi and Tadanori Morikawa and Teruzo Miyoshi and Kosuke Nishi and Michiko Wada and Hidetoshi Yamada and S. Ohshima A. Shimizu},
  journal={European journal of biochemistry},
  year={1997},
  volume={248 2},
  pages={385-93}
}
D-Threonine aldolase is an enzyme that catalyzes the cleavage of D-threonine into glycine and acetaldehyde. Its activity was found in several genera of bacteria such as Arthrobacter, Alcaligenes, Xanthomonas, and Pseudomonas, but not in yeasts or fungi. The enzyme was purified to homogeneity from one strain, Arthrobacter sp. DK-38. The enzyme appeared to consist of a single polypeptide chain with an apparent molecular mass of 51 kDa. This enzyme, as well as L-threonine aldolase, requires… CONTINUE READING