Abstract
Medium-ring lactones are synthetically challenging due to unfavorable energetics involved in cyclization. We have discovered a thioesterase enzyme DcsB, from the decarestrictine C1 (1) biosynthetic pathway, that efficiently performs medium-ring lactonizations. DcsB shows broad substrate promiscuity toward linear substrates that vary in lengths and substituents, and is a potential biocatalyst for lactonization. X-ray crystal structure and computational analyses provide insights into the molecular basis of catalysis.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Beauveria / enzymology
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Beauveria / genetics
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Biocatalysis
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Crystallography, X-Ray
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Cyclization
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Esterification
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Lactones / chemical synthesis*
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Lactones / metabolism
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Molecular Docking Simulation
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Multigene Family
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Protein Binding
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Substrate Specificity
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Thiolester Hydrolases / chemistry*
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Thiolester Hydrolases / genetics
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Thiolester Hydrolases / metabolism
Substances
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Fungal Proteins
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Lactones
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Thiolester Hydrolases