beta -Ketoacyl-Acyl Carrier Protein Synthase III (FabH) Is a Determining Factor in Branched-Chain Fatty Acid Biosynthesis

doi:10.1128/JB.182.2.365-370.2000

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Journal of Bacteriology, January 2000, p. 365-370, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

$beta$ -Ketoacyl-Acyl Carrier Protein Synthase III (FabH) Is a Determining Factor in Branched-Chain Fatty Acid Biosynthesis

Keum-Hwa Choi,¹ Richard J. Heath,¹ and Charles O. Rock¹^,²^,^*

Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105,¹ and Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163²

Received 11 August 1999/Accepted 27 October 1999

A universal set of genes encodes the components of the dissociated, type II, fatty acid synthase system that is responsiblefor producing the multitude of fatty acid structures found inbacterial membranes. We examined the biochemical basis for theproduction of branched-chain fatty acids by gram-positive bacteria.Two genes that were predicted to encode homologs of the $beta$ -ketoacyl-acylcarrier protein synthase III of Escherichia coli (eFabH) wereidentified in the Bacillus subtilis genome. Their protein productswere expressed, purified, and biochemically characterized. BothB. subtilis FabH homologs, bFabH1 and bFabH2, carried out theinitial condensation reaction of fatty acid biosynthesis withacetyl-coenzyme A (acetyl-CoA) as a primer, although they possessedlower specific activities than eFabH. bFabH1 and bFabH2 also utilizediso- and anteiso-branched-chain acyl-CoA primers as substrates.eFabH was not able to accept these CoA thioesters. Reconstitutionof a complete round of fatty acid synthesis in vitro with purifiedE. coli proteins showed that eFabH was the only E. coli enzymeincapable of using branched-chain substrates. Expression of eitherbFabH1 or bFabH2 in E. coli resulted in the appearance of a branched-chain17-carbon fatty acid. Thus, the substrate specificity of FabHis an important determinant of branched-chain fatty acidproduction.

^* Corresponding author. Mailing address: Department of Biochemistry, St. Jude Children's Research Hospital, 332 N. Lauderdale,Memphis, TN 38105-2794. Phone: (901) 495-3491. Fax: (901) 525-8025.E-mail: charles.rock{at}stjude.org.

Journal of Bacteriology, January 2000, p. 365-370, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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