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Enzymology of pyran ring A formation in salinomycin biosynthesis

Luhavaya, Hanna, Dias, Marcio V. B., Williams, Simon R., Hong, Hui, Gonzaga De Oliveira, Luciana and Leadlay, Peter F. 2015. Enzymology of pyran ring A formation in salinomycin biosynthesis. Angewandte Chemie International Edition 54 (46) , pp. 13622-13625. 10.1002/anie.201507090

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Tetrahydropyran rings are a common feature of complex polyketide natural products, but much remains to be learned about the enzymology of their formation. The enzyme SalBIII from the salinomycin biosynthetic pathway resembles other polyether epoxide hydrolases/cyclases of the MonB family, but SalBIII plays no role in the conventional cascade of ring opening/closing. Mutation in the salBIII gene gave a metabolite in which ring A is not formed. Using this metabolite in vitro as a substrate analogue, SalBIII has been shown to form pyran ring A. We have determined the X-ray crystal structure of SalBIII, and structure-guided mutagenesis of putative active-site residues has identified Asp38 and Asp104 as an essential catalytic dyad. The demonstrated pyran synthase activity of SalBIII further extends the impressive catalytic versatility of α+β barrel fold proteins.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Additional Information: This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Publisher: Wiley
ISSN: 1433-7851
Date of First Compliant Deposit: 10 November 2022
Last Modified: 05 May 2023 18:39

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