Production of vancomycin aglycone conjugated to a peptide carrier domain derived from a biosynthetic non-ribosomal peptide synthetase.
A method for attaching the vancomycin aglycone to a peptide carrier domain (PCD) is reported which involves reacting the apo-PCD produced in Escherichia coli with vancomycin aglycone-coenzyme A thioester, catalyzed by the phosphopantetheinyl transferase Sfp from Bacillus subtilis.
Vitali
Francesca
F
Institute of Organic Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Zerbe
Katja
K
Robinson
John A
JA
D001412:Bacillus subtilis / Q000201:enzymology; D002352:Carrier Proteins / Q000737:chemistry*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D003065:Coenzyme A / Q000737:chemistry; D004926:Escherichia coli; D008956:Models, Chemical; D010446:Peptide Fragments / Q000737:chemistry; D010453:Peptide Synthases / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D017855:Transferases (Other Substituted Phosphate Groups) / Q000737:chemistry; D014640:Vancomycin / Q000031:analogs & derivatives* / Q000138:chemical synthesis*
D002352:Carrier Proteins; D010446:Peptide Fragments; D014640:Vancomycin; D017855:Transferases (Other Substituted Phosphate Groups); D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase; D003065:Coenzyme A