Journal
CHEMISTRY & BIOLOGY
Volume 13, Issue 4, Pages 453-460Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2006.01.013
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- Biotechnology and Biological Sciences Research Council [BB/D018943/1] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BB/D018943/1] Funding Source: researchfish
- BBSRC [BB/D018943/1] Funding Source: UKRI
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Ionophoric polyethers are produced by the exquisitely stereoselective oxidative cyclization of a linear polyketide, probably via a triepoxide intermediate. We report here that deletion of either or both of the monBI and monBII genes from the monensin biosynthetic gene cluster gave strains that produced, in place of monensins A and B, a mixture of C-3-demethylmonensins and a number of minor components, including C-9-epimonensin A. All the minor components were efficiently converted into monensins by subsequent acid treatment. These data strongly suggest that epoxide ring opening and concomitant polyether ring formation are catalyzed by the MonB enzymes, rather than by the enzyme MonCII as previously thought. Consistent with this, homology modeling shows that the structure of MonB-type enzymes closely resembles the recently determined structure of limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis.
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