Abstract
A nonribosomal peptide synthetase-like enzyme (NRPS325) from Aspergillus terreus was reconstituted in vitro and was shown to synthesize thiopyrazines using an unprecedented mechanism. Substrate promiscuity of NRPS325 toward different amino acids and free thiols was explored to produce >60 different thiopyrazine compounds.
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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Aspergillus / enzymology*
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Molecular Structure
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Multigene Family
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Peptide Synthases / genetics
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Peptide Synthases / metabolism*
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Pyrans / chemical synthesis*
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Pyrans / metabolism
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Substrate Specificity
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Sulfhydryl Compounds / chemical synthesis*
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Sulfhydryl Compounds / metabolism
Substances
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Pyrans
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Sulfhydryl Compounds
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thiopyran
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Peptide Synthases