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Cited by 314

The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.

Nonribosomal biosynthesis of peptide antibiotics

KLEINKAUF, Horst, von DÖHREN, Hans·1990·European Journal of Biochemistry

Abstract

Peptide antibiotics are known to contain non‐protein amino acids, D‐amino acids, hydroxy acids, and other unusual constituents. In addition they may be modified by N‐methylation and cyclization reactions. Their biosynthetic origin has been connected in many cases to an enzymatic system referred to as the ‘thiotemplate multienzymic mechanism’. This mechanism includes the activation of the constituent residues as adenylates on the enzymic template, the acylation of specific template thiol groups, epimerization or N‐methylation at this thioester stage, and polymerization in the sequence directed by the multienzymic structure with the aid of 4′‐phosphopantetheine as a cofactor, including possible cyclization or terminal modification reactions. The reaction sequences leading to gramicidin S, tyrocidine, cyclosporine, bacitracin, polymyxin, actinomycin, enniatin, beauvericin, δ‐(L‐α‐aminoadipyl)‐L‐cysteinyl‐D‐valine and linear gramicidin are discussed. The structures of the multienzymes, their genetic organization, the biological functions of these peptides and results on related systems are discussed.

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Crossref · 10.1111/j.1432-1033.1990.tb19188.x

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Metadata

Authors
KLEINKAUF, H., & von DÖHREN, H.
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
1990-08
Volume
192
Issue
1
Pages
1-15
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
OpenAlex
W1996610802
Cited by
314
References
25
FWCI
16.91
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Nonribosomal biosynthesis of peptide antibiotics. https://app.cochat.ai/papers/10.1111/j.1432-1033.1990.tb19188.x
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KLEINKAUF, H., & von DÖHREN, H. (1990). Nonribosomal biosynthesis of peptide antibiotics. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1990.tb19188.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.