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Discovery, Biosynthesis, and Engineering of Lantipeptides

Aided by genome-mining strategies, knowledge of the prevalence and diversity of ribosomally synthesized natural products (RNPs) is rapidly increasing. Among these are the lantipeptides, posttranslationally modified peptides containing characteristic thioether cross-links imperative for bioactivity a... Full description

Journal Title: Annual review of biochemistry 2012, Vol.81 (1), p.479-505
Main Author: Knerr, Patrick J
Other Authors: van der Donk, Wilfred A
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Annual Reviews
ID: ISSN: 0066-4154
Link: https://www.ncbi.nlm.nih.gov/pubmed/22404629
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title: Discovery, Biosynthesis, and Engineering of Lantipeptides
format: Article
creator:
  • Knerr, Patrick J
  • van der Donk, Wilfred A
subjects:
  • Antimicrobial peptides
  • Bacteria - metabolism
  • Bacteriocins - chemistry
  • Bacteriocins - classification
  • Bacteriocins - genetics
  • Bacteriocins - metabolism
  • Biochemistry
  • Biological Products
  • Biosynthesis
  • Chemical compounds
  • Enzymes
  • Genetic aspects
  • Genetic Engineering
  • genome mining
  • Genomes
  • lantibiotic
  • leader peptide
  • Peptides
  • Peptides - chemistry
  • Peptides - classification
  • Peptides - genetics
  • Peptides - metabolism
  • Physiological aspects
  • Post-translational modification
  • posttranslational modification
  • Protein Processing, Post-Translational
  • ribosomally synthesized natural product
ispartof: Annual review of biochemistry, 2012, Vol.81 (1), p.479-505
description: Aided by genome-mining strategies, knowledge of the prevalence and diversity of ribosomally synthesized natural products (RNPs) is rapidly increasing. Among these are the lantipeptides, posttranslationally modified peptides containing characteristic thioether cross-links imperative for bioactivity and stability. Though this family was once thought to be a limited class of antimicrobial compounds produced by gram-positive bacteria, new insights have revealed a much larger diversity of activity, structure, biosynthetic machinery, and producing organisms than previously appreciated. Detailed investigation of the enzymes responsible for installing the posttranslational modifications has resulted in improved in vivo and in vitro engineering systems focusing on enhancement of the therapeutic potential of these compounds. Although dozens of new lantipeptides have been isolated in recent years, bioinformatic analyses indicate that many hundreds more await discovery owing to the widespread frequency of lantipeptide biosynthetic machinery in bacterial genomes.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 0066-4154
fulltext: fulltext
issn:
  • 0066-4154
  • 1545-4509
url: Link


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descriptionAided by genome-mining strategies, knowledge of the prevalence and diversity of ribosomally synthesized natural products (RNPs) is rapidly increasing. Among these are the lantipeptides, posttranslationally modified peptides containing characteristic thioether cross-links imperative for bioactivity and stability. Though this family was once thought to be a limited class of antimicrobial compounds produced by gram-positive bacteria, new insights have revealed a much larger diversity of activity, structure, biosynthetic machinery, and producing organisms than previously appreciated. Detailed investigation of the enzymes responsible for installing the posttranslational modifications has resulted in improved in vivo and in vitro engineering systems focusing on enhancement of the therapeutic potential of these compounds. Although dozens of new lantipeptides have been isolated in recent years, bioinformatic analyses indicate that many hundreds more await discovery owing to the widespread frequency of lantipeptide biosynthetic machinery in bacterial genomes.
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subjectAntimicrobial peptides ; Bacteria - metabolism ; Bacteriocins - chemistry ; Bacteriocins - classification ; Bacteriocins - genetics ; Bacteriocins - metabolism ; Biochemistry ; Biological Products ; Biosynthesis ; Chemical compounds ; Enzymes ; Genetic aspects ; Genetic Engineering ; genome mining ; Genomes ; lantibiotic ; leader peptide ; Peptides ; Peptides - chemistry ; Peptides - classification ; Peptides - genetics ; Peptides - metabolism ; Physiological aspects ; Post-translational modification ; posttranslational modification ; Protein Processing, Post-Translational ; ribosomally synthesized natural product
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abstractAided by genome-mining strategies, knowledge of the prevalence and diversity of ribosomally synthesized natural products (RNPs) is rapidly increasing. Among these are the lantipeptides, posttranslationally modified peptides containing characteristic thioether cross-links imperative for bioactivity and stability. Though this family was once thought to be a limited class of antimicrobial compounds produced by gram-positive bacteria, new insights have revealed a much larger diversity of activity, structure, biosynthetic machinery, and producing organisms than previously appreciated. Detailed investigation of the enzymes responsible for installing the posttranslational modifications has resulted in improved in vivo and in vitro engineering systems focusing on enhancement of the therapeutic potential of these compounds. Although dozens of new lantipeptides have been isolated in recent years, bioinformatic analyses indicate that many hundreds more await discovery owing to the widespread frequency of lantipeptide biosynthetic machinery in bacterial genomes.
copUnited States
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pmid22404629
doi10.1146/annurev-biochem-060110-113521