Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity.
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 showed that the extracts of polyamine-treated cells contain as much enzyme protein as normal cell extracts. This loss of ornithine decarboxylase activity is probably due to a post-translational modification of enzyme protein because we found no evidence for any inhibitor of activity in the polyamine-treated cells.[1]References
- Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity. Tyagi, A.K., Tabor, C.W., Tabor, H. J. Biol. Chem. (1981) [Pubmed]
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