Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity.

@article{Tyagi1981OrnithineDF,
  title={Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity.},
  author={Anil K Tyagi and Celia White Tabor and Herbert Tabor},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 23},
  pages={12156-63}
}
Ornithine decarboxylase has been purified 1,500-fold to homogeneity from a spe2 mutant of Saccharomyces cerevisiae which lacks S-adenosylmethionine decarboxylase and is derepressed for ornithine decarboxylase. The ornithine decarboxylase is a single polypeptide (Mr = 68,000) and requires a thiol and pyridoxal phosphate for activity. Addition of 10(-4) M spermidine and 10(-4) M spermine to the growth medium reduces the activity of the enzyme by 90% in 4 h. However, immunoprecipitation studies… CONTINUE READING