Dihydroxyacetone kinase from a methylotrophic yeast, Hansenula polymorpha CBS 4732

@article{Kato2004DihydroxyacetoneKF,
  title={Dihydroxyacetone kinase from a methylotrophic yeast, Hansenula polymorpha CBS 4732},
  author={Nobuo Kato and Hiroshi Yoshikawa and Katsuhiko Tanaka and Masayuki Shimao and Chikahiro Sakazawa},
  journal={Archives of Microbiology},
  year={2004},
  volume={150},
  pages={155-159}
}
Dihydroxyacetone (DHA) kinase was purified to electrophoretic homogeneity from methanol-grown Hansenula polymorpha CBS 4732. The enzyme was a dimer with a molecular weight of 150,000, and had an isoelectric point of 4.9. The enzyme was active toward DHA, and D- and L-glyceraldehydes as phosphorylation acceptors, and only ATP served as a donor. ADP inhibited… CONTINUE READING