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Journal of Bacteriology, February 2001, p. 1499-1503, Vol. 183, No. 4
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.4.1499-1503.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Inhibition of Escherichia coli Acetyl Coenzyme A Carboxylase by Acyl-Acyl Carrier Protein

Mark S. Davis1,dagger and John E. Cronan Jr.1,2,*

Departments of Microbiology1 and Biochemistry,2 University of Illinois, Urbana, Illinois 61801

Received 1 September 2000/Accepted 16 November 2000

Escherichia coli acetyl coenzyme A carboxylase (ACC), the first enzyme of the fatty acid biosynthetic pathway, is inhibited by acylated derivatives of acyl carrier protein (ACP). ACP lacking an acyl moiety does not inhibit ACC. Acylated derivatives of ACP having chain lengths of 6 to 20 carbon atoms were similarly inhibitory at physiologically relevant concentrations. The observed feedback inhibition was specific to the protein moiety, as shown by the inability of the palmitoyl thioester of spinach ACP I to inhibit ACC.

* Corresponding author. Mailing address: Department of Microbiology, University of Illinois, B103 Chemical and Life Sciences Laboratory, 601 S. Goodwin Ave., Urbana, IL 61801. Phone: (217) 333-7919. Fax: (217) 244-6697. E-mail: j-cronan{at}life.uiuc.edu.

dagger Present address: Biology Department, University of Evansville, Evansville, IN 47722.

Journal of Bacteriology, February 2001, p. 1499-1503, Vol. 183, No. 4
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.4.1499-1503.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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