Abstract
In vitro and in vivo characterization of the cyclomarin/cyclomarazine prenyltransferase CymD revealed its ability to prenylate tryptophan prior to incorporation into both cyclic peptides by the nonribosomal peptide synthetase CymA. This knowledge was utilized to bioengineer novel derivatives of these marine bacterial natural products by providing synthetic N-alkyl tryptophans to a prenyltransferase-deficient mutant of Salinispora arenicola CNS-205.
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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Actinobacteria / enzymology*
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Bioengineering
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Dimethylallyltranstransferase / deficiency
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Dimethylallyltranstransferase / metabolism*
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Marine Biology
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Molecular Structure
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Peptide Synthases
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Peptides, Cyclic / biosynthesis*
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / metabolism
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Tryptophan / analogs & derivatives*
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Tryptophan / biosynthesis*
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Tryptophan / chemistry
Substances
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Peptides, Cyclic
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Tryptophan
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Dimethylallyltranstransferase
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Peptide Synthases
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2,3-dihydroxybenzoate - serine ligase