Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae.
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.
D012437:Adenosylmethionine Decarboxylase / Q000378:metabolism*; D001894:Borohydrides / Q000494:pharmacology; D002262:Carboxy-Lyases / Q000378:metabolism*; D011773:Pyruvates / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D001894:Borohydrides; D011773:Pyruvates; D002262:Carboxy-Lyases; D012437:Adenosylmethionine Decarboxylase