Work

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

Year: 1970

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)63216-8

Authors: Reed B. Wickner, Celia White Tabor, Herbert Tabor

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

Language: English

Topic: Biochemical and Molecular Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1553727277

FWCI: 4.535

Cites: 35

Cited by: 160

Related to: 10