Addition/Correction Cite This: Biochemistry XXXX, XXX, XXX-XXX
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Correction to Radical S‑Adenosylmethionine Enzymes Involved in RiPP Biosynthesis Nilkamal Mahanta, Graham A. Hudson, and Douglas A. Mitchell* Biochemistry 2017, 56 (40), 5229−5244. DOI: 10.1021/acs.biochem.7b00771
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he sactionine linkages shown in the original Figure 7C for compounds 30 and 31 contained an error. The corrected figure shows that the sactionine linkages in Trnα (compound 30) are between Cys5 and Thr28, Cys9 and Thr25, and Cys13 and Ser21. The sactionines in Trnβ (compound 31) connect Cys5 to Tyr28, Cys9 to Ala25, and Cys13 to Thr21. This updated figure is now in accord with the associated text.
Figure 7. (A) Several RiPP BGCs have been identified that feature a rSAM responsible for sactionine installation. (B) Structure of a sactionine linkage. (C) Sactipeptides exhibit variations in the number and location of the sactionine linkages. An asterisk denotes sactionines observed only through in vitro reconstitution (i.e., the natural product has not been characterized). (D) Proposed mechanism for sactionine biosynthesis. (E) In contrast to the radicalbased mechanism of sactionine formation, lanthionines, which feature a Cβ thioether linkage, are formed through a Michael-type addition.
Received: October 18, 2017
© 2017 American Chemical Society
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DOI: 10.1021/acs.biochem.7b01056 Biochemistry XXXX, XXX, XXX−XXX
