Production of vancomycin aglycone conjugated to a peptide carrier domain derived from a biosynthetic non-ribosomal peptide synthetase

Francesca Vitali; Katja Zerbe; John A Robinson

doi:10.1039/b308247d

Production of vancomycin aglycone conjugated to a peptide carrier domain derived from a biosynthetic non-ribosomal peptide synthetase

Chem Commun (Camb). 2003 Nov 7:(21):2718-9. doi: 10.1039/b308247d.

Authors

Francesca Vitali¹, Katja Zerbe, John A Robinson

Affiliation

¹ Institute of Organic Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.

PMID: 14649827
DOI: 10.1039/b308247d

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillus subtilis / enzymology
Carrier Proteins / chemistry*
Catalysis
Chromatography, High Pressure Liquid
Coenzyme A / chemistry
Escherichia coli
Models, Chemical
Peptide Fragments / chemistry
Peptide Synthases / biosynthesis*
Peptide Synthases / chemistry*
Peptide Synthases / genetics
Transferases (Other Substituted Phosphate Groups) / chemistry
Vancomycin / analogs & derivatives*
Vancomycin / chemical synthesis*

Substances

Carrier Proteins
Peptide Fragments
Vancomycin
Transferases (Other Substituted Phosphate Groups)
Peptide Synthases
non-ribosomal peptide synthase
Coenzyme A