Studies on the quaternary structure of Escherichia coli pyruvate oxidase

• Published in: The Journal of biological chemistry Vol. 255; no. 2; pp. 379 - 383
• Main Authors: Stevens, D.J., Gennis, R.B.
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 25.01.1980
• Subjects: Azides; Cell Membrane - enzymology; Escherichia coli - enzymology; Macromolecular Substances; Naphthalenesulfonates; Protein Binding; Protein Conformation; Pyruvate Oxidase; Spectrometry, Fluorescence; Spectrophotometry

Pyruvate oxidase is a peripheral membrane enzyme isolated from Escherichia coli. The enzyme catalyzes the oxidative decarboxylation of pyruvate to yield acetate plus CO2. The specific activity of the purified oxidase is stimulated 25-fold by lipids, and this lipid requirement has been the subject of...