Structural highlights
Publication Abstract from PubMed
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.
Deciphering the late steps of rifamycin biosynthesis.,Qi F, Lei C, Li F, Zhang X, Wang J, Zhang W, Fan Z, Li W, Tang GL, Xiao Y, Zhao G, Li S Nat Commun. 2018 Jun 14;9(1):2342. doi: 10.1038/s41467-018-04772-x. PMID:29904078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qi F, Lei C, Li F, Zhang X, Wang J, Zhang W, Fan Z, Li W, Tang GL, Xiao Y, Zhao G, Li S. Deciphering the late steps of rifamycin biosynthesis. Nat Commun. 2018 Jun 14;9(1):2342. doi: 10.1038/s41467-018-04772-x. PMID:29904078 doi:http://dx.doi.org/10.1038/s41467-018-04772-x
