Partial Purification and Properties of Acyl‐CoA Synthetase of Escherichia coli

Abstract

A purification of acyl‐CoA synthetase of Escherichia coli is described. The enzyme behaves as an acid: CoA ligase (AMP) (EC 6.2.1.3), being active on C4–C18 fatty acids. A multienzyme complex (120000 molecular weight) seems to be involved; although the ratios of activities on different fatty acids remain constant during the purification procedure, heat treatment, kinetic experiments and column chromatography on hydroxyapatite indicate the presence of two enzymes, one acting on short and medium chain fatty acids, and the other on long chain fatty acids. Copyright © 1970, Wiley Blackwell. All rights reserved