Chin. J. Org. Chem. ›› 2018, Vol. 38 ›› Issue (9): 2377-2385.DOI: 10.6023/cjoc201806016 Previous Articles     Next Articles

Special Issue: 合成科学



沈洁洁a,b, 毛旭明a,b, 陈新爱a,b, 李永泉a,b   

  1. a 浙江大学药物生物技术研究所 杭州 310058;
    b 浙江省微生物生化与代谢工程重点实验室 杭州 310058
  • 收稿日期:2018-06-12 修回日期:2018-06-29 发布日期:2018-07-16
  • 通讯作者: 李永泉
  • 基金资助:


Recent Advances in Acyltransferase Domain of Type I Polyktide Synthases

Shen Jiejiea,b, Mao Xuminga,b, Chen Xin'aia,b, Li Yongquana,b   

  1. a Institute of Pharmaceutical Biotechnology, Zhejiang University, Hangzhou 310058;
    b Key Laboratory of Microbial Biochemistry and Metabolism Engineering of Zhejiang Province, Hangzhou 310058
  • Received:2018-06-12 Revised:2018-06-29 Published:2018-07-16
  • Contact: 10.6023/cjoc201806016
  • Supported by:

    Project supported by the National Natural Science Foundation of China (Nos. 3173002, 31520103901, 31470212, 31571284).

Most polyketide natural compounds, such as antibiotics, antineoplastics and immunosuppressants, are produced by type I polyketide synthases (PKSs). Type I PKSs are composed of several catalytic modules, each of which contains iterative domains, such as acyltransferase (AT) domain, for one round of polyketide chain elongation. The recent advances on AT domains of type I PKS modules and analyzes their categories, the diverse acyl subunits they transfer, their catalytic mechanisms and their protein structures are summarized. Moreover, the recent progress in AT engineering (AT domains swaps, AT site-directed mutagenesis and trans-AT complementation) for new polyketide derivatives is summarized, to show that the substrate specificity of AT domains is one of the key factors on determining the diversity of polyketide backbones. These works have laid a theoretical foundation for the further development of novel polyketides with multi-functions and in high-yields by AT domain engineering.

Key words: AT domain, substrate specificity, catalytic mechanism, type I PKS, polyketide