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The Journal of biological chemistry v.292 no.4, 2017년, pp.1374 - 1384   SCI SCIE
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Cyclic AMP Inhibits the Activity and Promotes the Acetylation of Acetyl-CoA Synthetase through Competitive Binding to the ATP/AMP Pocket

Han, Xiaobiao (From the Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China, ) ; Shen, Liqiang (the Key Laboratory of Synthetic Biology, Chinese Academy of Sciences Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China, ) ; Wang, Qijun (the Department of Medical Microbiology and Parasitology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China, ) ; Cen, Xufeng (From the Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China, ) ; Wang, Jin (From the Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China, ) ; Wu, Meng (the Shanghai Institute of Biochemistr ) ; Li, Peng ; Zhao, Wei ; Zhang, Yu ; Zhao, Guoping ;
  • 초록  

    The high-affinity biosynthetic pathway for converting acetate to acetyl-coenzyme A (acetyl-CoA) is catalyzed by the central metabolic enzyme acetyl-coenzyme A synthetase (Acs), which is finely regulated both at the transcriptional level via cyclic AMP (cAMP)-driven trans -activation and at the post-translational level via acetylation inhibition. In this study, we discovered that cAMP directly binds to Salmonella enterica Acs ( Se Acs) and inhibits its activity in a substrate-competitive manner. In addition, cAMP binding increases Se Acs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced Se Acs inhibition. A crystal structure study and site-directed mutagenesis analyses confirmed that cAMP binds to the ATP/AMP pocket of Se Acs, and restrains Se Acs in an open conformation. The cAMP contact residues are well conserved from prokaryotes to eukaryotes, suggesting a general regulatory mechanism of cAMP on Acs.


  • 주제어

    acetyl-CoA synthetase .   acetylation .   crystal structure .   cyclic AMP (cAMP) .   post-translational modification (PTM).  

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