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Originally published In Press as doi:10.1074/jbc.M208920200 on September 16, 2002

J. Biol. Chem., Vol. 277, Issue 47, 44809-44816, November 22, 2002
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A New Mechanism for Anaerobic Unsaturated Fatty Acid Formation in Streptococcus pneumoniae*

Hedia MarrakchiDagger , Keum-Hwa ChoiDagger §, and Charles O. RockDagger ||

From the Dagger  Department of Infectious Diseases, Protein Science Division, St Jude Children's Research Hospital, Memphis, Tennessee 38105 and the  Department of Molecular Biosciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163

The anaerobic pathway for unsaturated fatty acid synthesis was established in the 1960s in Escherichia coli. The double bond is introduced into the growing acyl chain by FabA, an enzyme capable of both the dehydration of beta -hydroxydecanoyl-acyl carrier protein (ACP) to trans-2-decenoyl-ACP, and the isomerization of trans-2 to cis-3-decenoyl-ACP. However, there are a number of anaerobic bacteria whose genomes do not contain a fabA homolog, although these organisms nonetheless produce unsaturated fatty acids. We cloned and biochemically characterized a new enzyme in type II fatty acid synthesis from Streptococcus pneumoniae that carries out the isomerization of trans-2-decenoyl-ACP to cis-3-decenoyl-ACP, but is not capable of catalyzing the dehydration of beta -hydroxy intermediates. This tetrameric enzyme, designated FabM, has no similarity to FabA, but rather is a member of the hydratase/isomerase superfamily. Thus, the branch point in the biosynthesis of unsaturated fatty acids in S. pneumoniae occurs following the formation of trans-2-decenoyl-ACP, in contrast to E. coli where the branch point takes place after the formation of beta -hydroxydecanoyl-ACP.


* This work was supported by National Institutes of Health Grant GM 34496, Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Syrian Associated Charities.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Division of Environmental Life Sciences, College of Natural Science, Seoul Women's University, Seoul, Korea 139-774.

|| To whom correspondence should be addressed: Dept. of Infectious Diseases, Protein Science Division, St Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Tel.: 901-495-3491; Fax: 901-495-3099; E-mail: charles.rock@stjude.org.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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