Deciphering the late steps of rifamycin biosynthesis

Feifei Qi, Chao Lei, Fengwei Li, Xingwang Zhang, Jin Wang, Wei Zhang, Zhen Fan, Weichao Li, Gong-Li Tang, Youli Xiao (), Guoping Zhao and Shengying Li ()
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Feifei Qi: Chinese Academy of Sciences
Chao Lei: Chinese Academy of Sciences
Fengwei Li: Chinese Academy of Sciences
Xingwang Zhang: Chinese Academy of Sciences
Jin Wang: Chinese Academy of Sciences
Wei Zhang: Chinese Academy of Sciences
Zhen Fan: Chinese Academy of Sciences
Weichao Li: Chinese Academy of Sciences
Gong-Li Tang: Chinese Academy of Sciences
Youli Xiao: Chinese Academy of Sciences
Guoping Zhao: Chinese Academy of Sciences
Shengying Li: Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract Rifamycin-derived drugs, including rifampin, rifabutin, rifapentine, and rifaximin, have long been used as first-line therapies for the treatment of tuberculosis and other deadly infections. However, the late steps leading to the biosynthesis of the industrially important rifamycin SV and B remain largely unknown. Here, we characterize a network of reactions underlying the biosynthesis of rifamycin SV, S, L, O, and B. The two-subunit transketolase Rif15 and the cytochrome P450 enzyme Rif16 are found to mediate, respectively, a unique C–O bond formation in rifamycin L and an atypical P450 ester-to-ether transformation from rifamycin L to B. Both reactions showcase interesting chemistries for these two widespread and well-studied enzyme families.

Date: 2018
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DOI: 10.1038/s41467-018-04772-x

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