Enzymological characterization of recombinant xenopus DG42, a vertebrate hyaluronan synthase.

@article{Pummill1998EnzymologicalCO,
  title={Enzymological characterization of recombinant xenopus DG42, a vertebrate hyaluronan synthase.},
  author={Philip E Pummill and Ann Mary Achyuthan and Paul L Deangelis},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 9},
  pages={4976-81}
}
We have characterized the hyaluronan (HA) synthase activity of the Xenopus DG42 gene product in vitro. The recombinant enzyme produced in yeast does not possess a nascent HA chain and, therefore, is an ideal model system for kinetic studies of the synthase's glycosyltransferase activity. The enzymatic rate was optimal from pH 7.6 to 8.1. Only the authentic sugar nucleotide precursors, UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylglucosamine (UDP-GlcNAc), were utilized to produce a large… CONTINUE READING

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