Chapter 19. In vitro studies of phenol coupling enzymes involved in vancomycin biosynthesis.
Oxidative phenol cross-linking reactions play a key role in the biosynthesis of glycopeptide antibiotics such as vancomycin. The vancomycin aglycone contains three cross-links between aromatic amino acid side-chains, which stabilize the folded backbone conformation required for binding to the target D-Ala-D-Ala dipeptide. At least the first cross-link is introduced into a peptide precursor whilst it is still bound as a thioester to a peptide carrier protein (PCP) domain (also called a thiolation domain) within the nonribosomal peptide synthetase. We described here methods for the solid-phase synthesis of peptides and their coupling to PCP domains, which may be useful for in vitro studies of cross-linking and related tailoring reactions during nonribosomal glycopeptide antibiotic biosynthesis.
Institute of Organic Chemistry, University of Zürich, Zürich, Switzerland.
Dong Bo
DB
Li
Katharina
K
Woithe
Nina
N
Geib
Khaled
K
Abou-Hadeed
Katja
K
Zerbe
John A
JA
Robinson
D019295:Computational Biology; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism; D005288:Ferredoxins / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D010452:Peptide Biosynthesis; D010453:Peptide Synthases / Q000378:metabolism; D014640:Vancomycin / Q000096:biosynthesis* / Q000737:chemistry
D005288:Ferredoxins; D014640:Vancomycin; D005287:Ferredoxin-NADP Reductase; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase