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Chapter 19. In vitro studies of phenol coupling enzymes involved in vancomycin biosynthesis


Li, D B; Woithe, K; Geib, N; Abou-Hadeed, K; Zerbe, K; Robinson, J A (2009). Chapter 19. In vitro studies of phenol coupling enzymes involved in vancomycin biosynthesis. In: Hopwood, D A. Complex Enzymes in Microbial Natural Product Biosynthesis, Part A: Overview Articles and Peptides. Amsterdam: Elsevier, 487-509.

Abstract

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.

Abstract

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.

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Additional indexing

Item Type:Book Section, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:2009
Deposited On:30 Dec 2009 09:01
Last Modified:05 Apr 2016 13:36
Publisher:Elsevier
Series Name:Methods in enzymology
ISSN:0076-6879
ISBN:9780123745880
Publisher DOI:https://doi.org/10.1016/S0076-6879(09)04819-8
Related URLs:http://opac.nebis.ch/F/?local_base=NEBIS&con_lng=GER&func=find-b&find_code=SYS&request=005830369
PubMed ID:19374995

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