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Noninvolvement of Acyl Carrier Protein with Citrate Synthase and Malate Synthase
Journal of Bacteriology
Acyl carrier protein (ACP coli) was isolated from commercially grown Escherichia coli B and was acetylated by chemical methods. Biological activity of the synthesized acetyl-ACP coli was checked in an in vitro fatty acid-synthesizing system isolated from E. coli B. Since acetyl-ACP is preferred over acetyl-coenzyme A (CoA) as a substrate in these reactions, the possibility that it may substitute for acetyl-CoA in biosynthetically and oxidatively important cellular pathways (glyoxylate and Krebsdoi:10.1128/jb.96.4.1281-1284.1968 fatcat:pwosedphhndvfa4wshejlrbzhe