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Journal of Chinese Pharmaceutical Sciences ›› 2015, Vol. 24 ›› Issue (3): 137-147.DOI: 10.5246/jcps.2015.03.017

• Review •     Next Articles

Advances of bacterial transferase MraY and its inhibitors

Yuanyuan Jin1#, Juanjuan Liu1,2#, Xiaozhou Feng1, Yadong Li1,2, Wan Sun1, Kangyou Wang1,2, Xifeng Tian2*, Zhaoyong Yang1*   

  1. 1. Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and  Peking Union Medical College, Beijing 100050, China
    2. Hebei United University, Tangshan 063000, China
  • Received:2014-11-05 Revised:2014-12-03 Online:2015-03-29 Published:2014-12-16
  • Contact: Tel.: 86-10-63165283
  • About author:Dr. Yang graduated from Institute of Medicinal Biotechnology Chinese Academy of Medical Sciences in 2003 and obtained his Ph.D. degree. During 2008–2011, he did postdoctoral research at University of Kentucky. In December 2011, he joined the Institute of Medicinal Biotechnology Chinese Academy of Medical Sciences as a Professor. His research interest is the identification of enzyme with novel catalytic mechanism in the natural product biosynthesis pathway, and to be applied in practice, in order to complete the enzymatic synthesis of pharmaceutical intermediates of significance.
  • Supported by:
    National Natural Science Foundation of China (Grant No. 81273414 and Grant No. 81321004), NSFC-NIH International Cooperation and Exchange Programs (Grant No. 81261120417, 2012-2013).

Abstract:

The phospho-murNAc-pentapeptide translocase (MraY, translocase I) is a good target for the development of new antibiotics as it is ubiquitous and essential for bacterial growth. Furthermore, several inhibitors targeting towards this enzyme have been discovered. Recently, the crystal structure of MraY has been presented by Chung et al. Combination of the crystal structure and structure-activity relationship studies on these inhibitors could lead to the identification of active pharmacophores, and insight into their mechanisms of action. In this review, we described the structure and inhibitors of MraY. In addition, we also discussed the structure-activity relationship of these inhibitors and prospects of MraY as an antibacterial target.

Key words: Peptidoglycan, MraY, Antibiotic, Structure-activity relationships

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