Purification of Adenosylmethionine Decarboxylase from Escherichia coli W: Evidence For Covalently Bound Pyruvate

Abstract

Abstract Adenosylmethionine decarboxylase has been purified 800-fold from extracts of Escherichia coli W. This preparation, which was homogeneous by sedimentation equilibrium experiments and by analytical disc gel electrophoresis, had a molecular weight of approximately 113,000 and a subunit molecular weight of 15,000. The enzymatic activity is abolished by carbonyl reagents. Based on the spectrum of the enzyme following reaction with phenylhydrazine, and on the recovery of 3H-lactate from hydrolysates of borotritide-reduced enzyme, covalently bound pyruvate has been identified as the carbonyl moiety involved in the enzymatic activity. There are 1 to 2 moles of pyruvate present per mole of enzyme.