{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T13:43:37Z","timestamp":1791899017376,"version":"4.3.4"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"13","license":[{"start":{"date-parts":[[2006,7,1]],"date-time":"2006-07-01T00:00:00Z","timestamp":1151712000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2006,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Acyl carrier protein (ACP) synthase (AcpS) catalyzes the transfer of the 4\u2032-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\n            <jats:italic>Escherichia coli<\/jats:italic>\n            ,\n            <jats:italic>Streptococcus pneumoniae<\/jats:italic>\n            , and\n            <jats:italic>Mycoplasma pneumoniae<\/jats:italic>\n            , 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\n            <jats:italic>M. pneumoniae<\/jats:italic>\n            , like\n            <jats:italic>E. coli<\/jats:italic>\n            enzyme, exhibits a homodimeric structure, but the enzyme from\n            <jats:italic>S. pneumoniae<\/jats:italic>\n            exhibits a trimeric structure. Our biochemical studies show that the AcpS enzymes from\n            <jats:italic>M. pneumoniae<\/jats:italic>\n            and\n            <jats:italic>S. pneumoniae<\/jats:italic>\n            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\n            <jats:italic>E. coli<\/jats:italic>\n            can utilize short-chain CoA derivatives but not the long-chain CoA derivatives tested. Finally, our biochemical studies show that\n            <jats:italic>M. pneumoniae<\/jats:italic>\n            AcpS is kinetically a very sluggish enzyme compared with those from\n            <jats:italic>E. coli<\/jats:italic>\n            and\n            <jats:italic>S. pneumoniae<\/jats:italic>\n            . 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.\n          <\/jats:p>","DOI":"10.1128\/jb.01917-05","type":"journal-article","created":{"date-parts":[[2006,6,20]],"date-time":"2006-06-20T23:15:17Z","timestamp":1150845317000},"page":"4737-4748","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":34,"title":["Acyl Carrier Protein Synthases from Gram-Negative, Gram-Positive, and Atypical Bacterial Species: Biochemical and Structural Properties and Physiological Implications"],"prefix":"10.1128","volume":"188","author":[{"given":"Kelly A.","family":"McAllister","sequence":"first","affiliation":[{"name":"Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert B.","family":"Peery","sequence":"additional","affiliation":[{"name":"Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Genshi","family":"Zhao","sequence":"additional","affiliation":[{"name":"Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"e_1_3_2_3_2","unstructured":"Baltz R. 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