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Liu W., Shen B. Genes for production of the enediyne antitumor antibiotic C-1027 in Streptomyces globisporus are clustered with the cagA gene that encodes the C-1027 apoprotein. Antimicrob. Agent Chemother. 44:2000;382-392.
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Zhu G., LaGier M.J., Stejskal F., Millership J.J., Cai X., Keithly J.S. Cryptosporidium parvum: the first protist known to encode a putative polyketide synthase. Gene. 298:2002;79-89 Cloning and sequence analysis of a putative 'AT-less' PKS from the parasitic protist C. parvum is described. Neither the role of this cluster nor the functions of the gene product were known.
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Cloning and sequence analysis of the putative pederin biosynthetic gene cluster from an uncultured bacterial symbiont of Paederus beetles was described, revealing the pedFGH 'AT-less' PKS genes and pedCD discrete AT genes. Its involvement in pederin biosynthesis was based on sequence prediction only
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Piel J. A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles. Proc. Natl. Acad Sci. USA. 98:2002;14808-14813 Cloning and sequence analysis of the putative pederin biosynthetic gene cluster from an uncultured bacterial symbiont of Paederus beetles was described, revealing the pedFGH 'AT-less' PKS genes and pedCD discrete AT genes. Its involvement in pederin biosynthesis was based on sequence prediction only.
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Heterologous expression of the 23-gene non cluster is described, and resulted in the production of macrotetrolides. These results confirmed that macrotetrolide biosynthesis involves a type II PKS lacking ACP
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Kwon H.-J., Smith W.C., Xiang L., Shen B. Cloning and heterologous expression of the macrotetrolide biosynthetic gene cluster revealed a novel polyketide synthase that lacks an acyl carrier protein. J. Am. Chem. Soc. 123:2001;3385-3386 Heterologous expression of the 23-gene non cluster is described, and resulted in the production of macrotetrolides. These results confirmed that macrotetrolide biosynthesis involves a type II PKS lacking ACP.
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In vivo genetic, mutagenetic and in vitro biochemical studies of macrotetrolide biosynthesis are described. These results established that NonJK catalyse the C-O bond-forming cyclotetramerization steps and utilize acyl CoAs as substrates directly, revealing an unprecedented enzyme activity for PKS
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Kwon H.-J., Smith W.C., Scharon A.J., Hwang S.H., Kurth M.J., Shen B. C-O bond formation by polyketide synthases. Science. 297:2002;1327-1330 In vivo genetic, mutagenetic and in vitro biochemical studies of macrotetrolide biosynthesis are described. These results established that NonJK catalyse the C-O bond-forming cyclotetramerization steps and utilize acyl CoAs as substrates directly, revealing an unprecedented enzyme activity for PKS.
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A critical review of macrotetrolide biosynthesis emphasizes how early studies inspired effort that eventually led to the discovery of a novel PKS
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Shen B., Kwon H.-J. Macrotetrolide biosynthesis: a novel type II polyketide synthase. Chem. Rec. 2:2002;389-396 A critical review of macrotetrolide biosynthesis emphasizes how early studies inspired effort that eventually led to the discovery of a novel PKS.
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Structural modeling and site-directed mutagenesis of the actinorhodin β-ketoacyl-acyl carrier protein synthase
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Dissection of malonyl-CoA decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase
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Jez J.M., Ferrer J.-L., Bowman M.E., Dixon R.A., Noel J.P. Dissection of malonyl-CoA decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry. 39:2000;890-902.
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Production of polyunsaturated fatty acids by polyketide synthase in both prokaryotes and eukaryotes
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Polyunsaturated fatty acid biosynthetic pathways were cloned from a marine bacteria Shewanella and a marine protist Schizochytrium, respectively, revealing that they were biosynthesized by PKSs with distinct mechanism and structure. Their role in polyunsaturated fatty acid biosynthesis was confirmed by heterologous expression. In addition to the examples discussed in the text, these PKSs demonstrated yet another diversity in polyketide biosynthesis
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Metz J.G., Roessler P., Facciotti D., Levering C., Dittrich F., Lassner M., Valentine R., Lardizabal K., Domergue F., Yamada A.et al. Production of polyunsaturated fatty acids by polyketide synthase in both prokaryotes and eukaryotes. Science. 293:2001;290-293 Polyunsaturated fatty acid biosynthetic pathways were cloned from a marine bacteria Shewanella and a marine protist Schizochytrium, respectively, revealing that they were biosynthesized by PKSs with distinct mechanism and structure. Their role in polyunsaturated fatty acid biosynthesis was confirmed by heterologous expression. In addition to the examples discussed in the text, these PKSs demonstrated yet another diversity in polyketide biosynthesis.
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(2001)
Science
, vol.293
, pp. 290-293
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Metz, J.G.1
Roessler, P.2
Facciotti, D.3
Levering, C.4
Dittrich, F.5
Lassner, M.6
Valentine, R.7
Lardizabal, K.8
Domergue, F.9
Yamada, A.10
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