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The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins

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Abstract

Phosphopantetheinyl transferases (PPTases) catalyze the posttranslational modification of acyl carrier proteins (ACPs) in fatty acid synthases (FASs), ACPs in polyketide synthases, and peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs) in all organisms. Some bacterial PPTases have broad substrate specificities for ACPs/PCPs and/or coenzyme A (CoA)/CoA analogs, facilitating their application in metabolite production in hosts and/or labeling of ACPs/PCPs, respectively. Here, a group II PPTase SchPPT from Streptomyces chattanoogensis L10 was characterized to accept a heterologous ACP and acetyl-CoA. Thus, SchPPT is a promiscuous PPTase and may be used on polyketide production in heterologous bacterial host and labeling of ACPs.

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Acknowledgments

This work was supported by Zhejiang Provincial Natural Science Foundation of China LR16H300001 and LZ12C01001, National Natural Science Foundation of China 31200600 and 31470212, and National High Technology Research & Development Program of China (863 Program) 2012AA02A706 and 2012AA022107.

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Correspondence to Hui Jiang.

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Communicated by Erko Stackebrandt.

Yue-Yue Wang and Hong-Dou Luo have contributed equally.

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Wang, YY., Luo, HD., Zhang, XS. et al. The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins. Arch Microbiol 198, 193–197 (2016). https://doi.org/10.1007/s00203-015-1179-z

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  • DOI: https://doi.org/10.1007/s00203-015-1179-z

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