{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T09:13:31Z","timestamp":1778922811694,"version":"3.51.4"},"reference-count":47,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2004,11,1]],"date-time":"2004-11-01T00:00:00Z","timestamp":1099267200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Lipids"],"published-print":{"date-parts":[[2004,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The increasing of multidrug resistance of clinically important pathogens calls for the development of novel antibiotics with unexploited cellular targets. FA biosynthesis in bacteria is catalyzed by a group of highly conserved proteins known as the type II FA synthase (FAS II) system. Bacteria FAS II organization is distinct from its mammalian counterpart; thus the FAS II pathway offers several unique steps for selective inhibition by antibacterial agents. Some known antibiotics that target the FAS II system include triclosan, isoniazid, and thiolactomycin. Recent years have seen remarkable progress in the understanding of the genetics, biochemistry, and regulation of the FAS II system with the availability of the complete geome, sequence for many bacteria. Crystal structures of the FAS II pathway enzymes have been determined for not only the <jats:italic>Escherichia coli<\/jats:italic> model system but also other gram\u2010netative and gram\u2010positive pathogens. The protein structures have greatly facilitated structure\u2010based design of novel inhibitors and the improvement of existing antibacterial agents. This review discusses new developments in the discovery of inhibitors that specifically target the two reductase steps of the FAS II system, \u03b2\u2010ketoacyl\u2010acyl carrier potein (ACP) reductase and enoyl\u2010ACP reductase.<\/jats:p>","DOI":"10.1007\/s11745-004-1330-3","type":"journal-article","created":{"date-parts":[[2006,12,18]],"date-time":"2006-12-18T10:49:26Z","timestamp":1166438966000},"page":"1055-1060","source":"Crossref","is-referenced-by-count":66,"title":["The reductase steps of the type II fatty acid synthase as antimicrobial targets"],"prefix":"10.1002","volume":"39","author":[{"given":"Yong\u2010Mei","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Infectious Diseases, Protein Science Division St. Jude Children's Research Hospital 332 N. Lauderdale Memphis TN 38105\u20102794"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying\u2010Jie","family":"Lu","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, Protein Science Division St. Jude Children's Research Hospital 332 N. Lauderdale Memphis TN 38105\u20102794"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Charles O.","family":"Rock","sequence":"additional","affiliation":[{"name":"Department of Molecular Sciences University of Tennessee Health Science Center Memphis Tennessee 38163"},{"name":"Department of Infectious Diseases, Protein Science Division St. Jude Children's Research Hospital 332 N. 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