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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
A New Mechanism for Anaerobic Unsaturated Fatty Acid Formation in
Streptococcus pneumoniae*
Hedia
Marrakchi ,
Keum-Hwa
Choi §, and
Charles O.
Rock ¶
From the 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 -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 -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
-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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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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