The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: Genetic and enzymological characterization

doi:10.1074/jbc.M505736200

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Papers In Press, published online ahead of print August 17, 2005
J. Biol. Chem, 10.1074/jbc.M505736200
Submitted on May 25, 2005
Revised on August 16, 2005
Accepted on August 17, 2005

The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: Genetic and enzymological characterization

Jacob Thomas and John E. Cronan . Jr

Microbiology Dept., University of Illinois, Urbana, IL 61801

Corresponding Author: j-cronan{at}life.uiuc.edu

The acyl carrier proteins (ACPs) of fatty acid synthesis are functional only when modified by attachment of the prosthetic group, 4'-phosphopanthetheine (4’-PP), that is transferred from CoA to the hydroxyl group of a specific serine residue. Almost forty years ago Vagelos and Larabee (Vagelos, PR and Larrabee, A (1967). J Biol Chem 242, 1776-1781) reported an enzyme from Escherichia coli that removed the prosthetic group. We report that this enzyme, called ACP hydroylase or ACP phosphodiesterase, is encoded by a gene (yajB) of previously unknown function that we have renamed acpH. A mutant E. coli strain having a total deletion of the acpH gene has been constructed that grows normally, showing that phosphodiesterase activity is not essential for growth, although it is required for turnover of the ACP prosthetic group in vivo. ACP phosphodiesterase (AcpH) has been purified to homogeneity for the first time and is a soluble protein that very readily aggregates upon over-expression in vivo or concentration in vitro. The purified enzyme has been shown to cleave acyl-ACP species with acyl chains of 6-16 carbon atoms and is active on some, but not all, non-native ACP species tested. Possible physiological roles for AcpH are discussed

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