The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier protei
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ORIGINAL PAPER
The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins Yue‑Yue Wang1 · Hong‑Dou Luo1 · Xiao‑Sheng Zhang1 · Tao Lin2 · Hui Jiang1 · Yong‑Quan Li1
Received: 29 September 2015 / Revised: 24 November 2015 / Accepted: 9 December 2015 / Published online: 9 January 2016 © Springer-Verlag Berlin Heidelberg 2016
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. Keywords Phosphopantetheinyl transferases · Substrate specificity · Acyl carrier protein · Streptomyces chattanoogensis · Coenzyme A
Introduction Phosphopantetheinyl transferases (PPTases) play an essential role in the biosyntheses of fatty acids, polyketides, and nonribosomal peptides in all organisms. In vivo function Communicated by Erko Stackebrandt. Yue-Yue Wang and Hong-Dou Luo have contributed equally. * Hui Jiang [email protected] 1
College of Life Sciences, Zhejiang University, Hangzhou 310058, Zhejiang, China
2
Shanghai Aobopharmtech Inc. Ltd., Shanghai 201203, China
of PPTases is to catalyze posttranslational modification of acyl carrier proteins (ACPs) in fatty acid synthases (FASs), ACPs in polyketide synthases (PKSs), and peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs) (Walsh et al. 1997; Sunbul et al. 2009; Beld et al. 2014; Wang et al. 2014). PPTases can be classified into three groups based on their structures. Both group I PPTases (ACPS-type PPTases) and group II PPTases (Sfptype PPTases) are discrete PPTases; however, group III PPTases exist as domains within PKSs or FASs (Sanchez et al. 2001; Weissman et al. 2004; Huang et al. 2006; Meiser and Muller 2008; Murugan and Liang 2008). Some bacterial PPTases have been known to be necessary in heterologous production of polyketides and nonribosomal peptides in microbial hosts (Ku et al. 1997; Hauvermale et al. 2006; Jiang et al. 2008). In most bacteria, the number of discrete PPTases is much less than the number of PCPs/ACPs, supporting that one PPTases should accept many ACPs/PCPs (Mootz et al. 2001; Weissman et al. 2004; Lu et al. 2008; Jiang et al. 2013). Notably, a few PPTases with broad substrate specificities for ACPs/PCPs have been used on heterologous metabolite production (Gokhale et al. 1999). For example, expression of a fungal PKS (6-methylsalicylic acid synt
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