Work

Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae.

Year: 1977

Type: article

Abstract: S-Adenosylmethionine decarboxylase from Saccharomyces cerevisiae has been purified to homogeneity. Acid hydrolysis of NaB3H4-reduced enzyme released 2.2 mol of tritiated lactate per mol of dimeric enzyme, indicating that a pyruvate moiety is present. Inhibition of enzymatic activity by NaBH4 reduction and by carbonyl-binding reagents indicates that this pyruvoyl residue is required for the activity of the enzyme. This is the first example reported of a eukaryotic enzyme containing a covalently linked pyruvoyl residue.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)40957-4

Authors: M.S. Cohn, C.W. Tabor, H. Tabor

Institutions: National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases

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: W1528264954

FWCI: 0.925

Cites: 29

Cited by: 59

Related to: 10