Abstract
Iterative highly reducing polyketide synthases from filamentous fungi are the most complex and enigmatic type of polyketide synthase discovered to date. Here we uncover an unusual degree of programming by the hypothemycin highly reducing polyketide synthase, in which a single ketoreductase domain shows stereospecificity that is controlled by substrate length. Mapping of the structural domains responsible for this feature allowed for the biosynthesis of an unnatural diastereomer of the natural product dehydrozearalenol.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Fungi / enzymology
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Molecular Sequence Data
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NADP / metabolism
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Polyketide Synthases / chemistry*
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Polyketide Synthases / metabolism*
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Protein Structure, Tertiary
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Stereoisomerism
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Substrate Specificity
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Zearalenone / analogs & derivatives
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Zeranol / analogs & derivatives
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Zeranol / chemistry
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Zeranol / metabolism
Substances
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Fungal Proteins
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Recombinant Proteins
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hypothemycin
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NADP
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Zearalenone
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Zeranol
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Polyketide Synthases
Associated data
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PubChem-Substance/134337197
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PubChem-Substance/134337198
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PubChem-Substance/134337199
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PubChem-Substance/134337200
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PubChem-Substance/134337201
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PubChem-Substance/134337202
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PubChem-Substance/134337203
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PubChem-Substance/134337204
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PubChem-Substance/134337205
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PubChem-Substance/134337206
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PubChem-Substance/134337207
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PubChem-Substance/134337208
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PubChem-Substance/134337209
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PubChem-Substance/134337210
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PubChem-Substance/134337211
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PubChem-Substance/134337212
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PubChem-Substance/134337213
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PubChem-Substance/134337214
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PubChem-Substance/134337215
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PubChem-Substance/134337216
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PubChem-Substance/134337217
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PubChem-Substance/134337218
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PubChem-Substance/134337219
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PubChem-Substance/134337220