Work

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

Year: 1981

Type: article

Abstract: 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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)43247-4

Authors: A.K. Tyagi, C.W. Tabor, H. Tabor

Institutions: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases, Leo Pharma (Denmark)

Language: English

Topic: Polyamine Metabolism and Applications

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1601873895

FWCI: 2.654

Cites: 43

Cited by: 68

Related to: 10