Novel diketopiperazine metabolism in a microorganism: two-step hydrolysis of cyclo(Gly-Leu) to amino acids and preliminary characterization of cyclo(Gly-Leu) hydrolase and dipeptidase.

@article{Kanzaki2000NovelDM,
  title={Novel diketopiperazine metabolism in a microorganism: two-step hydrolysis of cyclo(Gly-Leu) to amino acids and preliminary characterization of cyclo(Gly-Leu) hydrolase and dipeptidase.},
  author={Hiroshi Kanzaki and Naomi Mizuta and Teruhiko Nitoda and Kazuyoshi Kawazu},
  journal={Journal of bioscience and bioengineering},
  year={2000},
  volume={89 6},
  pages={602-5}
}
A bacterium, strain NM 5-3, isolated from soil exhibited the highest cyclo(Gly-Leu) (CGL)-hydrolyzing activity and was identified as Agrobacterium radiobacter. The reaction products from CGL were dipeptides (Leu-Gly and Gly-Leu) and amino acids (Leu and Gly). Inhibitors for the dipeptidase of this strain did not inhibit the hydrolysis of CGL to dipeptides, indicating that two distinct enzymes, CGLase and a dipeptidase, were involved in its hydrolysis. The activities of these two enzymes were… CONTINUE READING