Hollenhorst, Marie A.; Bumpus, Stefanie B.; Matthews, Megan L.; Bollinger, J. Martin Jr.; Kelleher, Neil L.; Walsh, Christopher T. published the artcile< The Nonribosomal Peptide Synthetase Enzyme DdaD Tethers Nβ-Fumaramoyl-L-2,3-diaminopropionate for Fe(II)/α-Ketoglutarate-Dependent Epoxidation by DdaC during Dapdiamide Antibiotic Biosynthesis>, Recommanded Product: (S)-tert-Butyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate, the main research area is Pantoea nonribosomal peptide synthetase DdaD epoxidation DdaC DdaF dapdiamide.
The gene cluster from Pantoea agglomerans responsible for biosynthesis of the dapdiamide antibiotics encodes an adenylation-thiolation didomain protein, DdaD, and an Fe(II)/α-ketoglutarate-dependent dioxygenase homolog, DdaC. Here we show that DdaD, a nonribosomal peptide synthetase module, activates and sequesters Nβ-fumaramoyl-L-2,3-diaminopropionate as a covalently tethered thioester for subsequent oxidative modification of the fumaramoyl group. DdaC catalyzes Fe(II)- and α-ketoglutarate-dependent epoxidation of the covalently bound Nβ-fumaramoyl-L-2,3-diaminopropionyl-S-DdaD species to generate Nβ-epoxysuccinamoyl-DAP (DAP = 2,3-diaminopropionate) in thioester linkage to DdaD. After hydrolytic release, Nβ-epoxysuccinamoyl-DAP can be ligated to L-valine by the ATP-dependent ligase DdaF to form the natural antibiotic Nβ-epoxysuccinamoyl-DAP-Val.
Journal of the American Chemical Society published new progress about Antibiotics (dapdiamide). 77215-54-4 belongs to class esters-buliding-blocks, and the molecular formula is C12H24N2O4, Recommanded Product: (S)-tert-Butyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate.
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