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

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• 作者：Yue-Yue Wang ; Hong-Dou Luo ; Xiao-Sheng Zhang ; Tao Lin…
• 关键词：Phosphopantetheinyl transferases ; Substrate specificity ; Acyl carrier protein ; Streptomyces chattanoogensis ; Coenzyme A
• 刊名：Archives of Microbiology
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：198
• 期：2
• 页码：193-197
• 全文大小：815 KB
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• 作者单位：Yue-Yue Wang (1)
  Hong-Dou Luo (1)
  Xiao-Sheng Zhang (1)
  Tao Lin (2)
  Hui Jiang (1)
  Yong-Quan Li (1)
  
  1. College of Life Sciences, Zhejiang University, Hangzhou, 310058, Zhejiang, China
  2. Shanghai Aobopharmtech Inc. Ltd., Shanghai, 201203, China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Microbial Ecology
  Biochemistry
  Cell Biology
  Biotechnology
  Ecology
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1432-072X

文摘

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