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Journal of Bacteriology, July 2006, p. 4737-4748, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.01917-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Acyl Carrier Protein Synthases from Gram-Negative, Gram-Positive, and Atypical Bacterial Species: Biochemical and Structural Properties and Physiological Implications

Kelly A. McAllister, Robert B. Peery, and Genshi Zhao*

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285

Received 15 December 2005/ Accepted 21 April 2006

Acyl carrier protein (ACP) synthase (AcpS) catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A (CoA) onto a serine residue of apo-ACP, resulting in the conversion of apo-ACP to the functional holo-ACP. The holo form of bacterial ACP plays an essential role in mediating the transfer of acyl fatty acid intermediates during the biosynthesis of fatty acids and phospholipids. AcpS is therefore an attractive target for therapeutic intervention. In this study, we have purified and characterized the AcpS enzymes from Escherichia coli, Streptococcus pneumoniae, and Mycoplasma pneumoniae, which exemplify gram-negative, gram-positive, and atypical bacteria, respectively. Our gel filtration column chromatography and cross-linking studies demonstrate that the AcpS enzyme from M. pneumoniae, like E. coli enzyme, exhibits a homodimeric structure, but the enzyme from S. pneumoniae exhibits a trimeric structure. Our biochemical studies show that the AcpS enzymes from M. pneumoniae and S. pneumoniae can utilize both short- and long-chain acyl CoA derivatives but prefer long-chain CoA derivatives as substrates. On the other hand, the AcpS enzyme from E. coli can utilize short-chain CoA derivatives but not the long-chain CoA derivatives tested. Finally, our biochemical studies show that M. pneumoniae AcpS is kinetically a very sluggish enzyme compared with those from E. coli and S. pneumoniae. Together, the results of these studies show that the AcpS enzymes from different bacterial species exhibit different native structures and substrate specificities with regard to the utilization of CoA and its derivatives. These findings suggest that AcpS from different microorganisms plays a different role in cellular physiology.

* Corresponding author. Mailing address: Lilly Research Laboratories, Cancer Research, DC 0434, Eli Lilly and Company, Indianapolis, IN 46285. Phone: (317) 276-2040. Fax: (317) 276-1414. E-mail: zhao_genshi{at}lilly.com.

Journal of Bacteriology, July 2006, p. 4737-4748, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.01917-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gong, H., Murphy, A., McMaster, C. R., Byers, D. M. (2007). Neutralization of Acidic Residues in Helix II Stabilizes the Folded Conformation of Acyl Carrier Protein and Variably Alters Its Function with Different Enzymes. J. Biol. Chem. 282: 4494-4503 [Abstract] [Full Text]  


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