| Literature DB >> 25413605 |
Yue-Yue Wang1, Xiao-Sheng Zhang, Ni-Ni Ren, Yuan-Yang Guo, Xin-Hang Jiang, Hui Jiang, Yu-Dong Li, Yong-Quan Li.
Abstract
It is known that bacterial group II phosphopantetheinyl transferases (PPTases) usually phosphopantetheinylate acyl carrier proteins (ACPs) involved in the secondary metabolism. For example, a bacterial group II PPTase SchPPT has been known to phosphopantetheinylate only ACPs involved in secondary metabolism, such as scn ACP0-2 and scn ACP7. In this study, we found two bacterial group II PPTases, Hppt and Sppt, could phosphopantetheinylate not only scn ACP0-2 and scn ACP7, but also sch FAS ACP, an ACP involved in primary metabolism. Swapping of the N terminus and C terminus of PPTases showed that (i) both the hybrids Hppt-Sppt and Sppt-Hppt could phosphopantetheinylate sch FAS ACP but not scn ACP0-2; (ii) both the hybrids Sppt-SchPPT and SchPPT-Sppt lost abilities to phosphopantetheinylate sch FAS ACP and scn ACP0-2. Hppt and Sppt represent group II PPTases which phosphopantetheinylate both ACPs involved in primary metabolism and ACPs involved in secondary metabolism.Entities:
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Year: 2014 PMID: 25413605 DOI: 10.1007/s00284-014-0735-0
Source DB: PubMed Journal: Curr Microbiol ISSN: 0343-8651 Impact factor: 2.188