Nonribosomal peptide synthesis definitely working out of the rules

Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called nonribosomal peptide synthetases. These synthetases are organized in modules constituted of adenylation, thiolation, and condensation core domains. As such, each module governs, according to the collinearity rule, the incorporation of a monomer within the growing peptide. The release of the peptide from the assembly chain is finally performed by a terminal core thioesterase domain. Secondary domains with modifying catalytic activities such as epimerization or methylation are sometimes included in the assembly lines as supplementary domains. This assembly line structure is analyzed by bioinformatics tools to predict the sequence and structure of the final peptides according to the sequence of the corresponding synthetases. However, a constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribosomal peptides. In this review, through several examples, we aim at highlighting these noncanonical pathways in order for the readers to perceive their complexity.

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Main Authors: Duban, Matthieu, Cociancich, Stéphane, Leclère, Valérie
Format: article biblioteca
Language:eng
Subjects:F60 - Physiologie et biochimie végétale, C30 - Documentation et information, peptide synthetase, peptide, polypeptide, biosynthèse, métabolite secondaire, bioinformatique, technique de prévision, synthèse, bibliographie, http://aims.fao.org/aos/agrovoc/c_13231, http://aims.fao.org/aos/agrovoc/c_5691, http://aims.fao.org/aos/agrovoc/c_27801, http://aims.fao.org/aos/agrovoc/c_928, http://aims.fao.org/aos/agrovoc/c_34335, http://aims.fao.org/aos/agrovoc/c_37958, http://aims.fao.org/aos/agrovoc/c_3041, http://aims.fao.org/aos/agrovoc/c_3def4163, http://aims.fao.org/aos/agrovoc/c_1335513885866,
Online Access:http://agritrop.cirad.fr/600447/
http://agritrop.cirad.fr/600447/1/microorganisms-10-00577.pdf
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spelling dig-cirad-fr-6004472024-01-29T19:06:14Z http://agritrop.cirad.fr/600447/ http://agritrop.cirad.fr/600447/ Nonribosomal peptide synthesis definitely working out of the rules. Duban Matthieu, Cociancich Stéphane, Leclère Valérie. 2022. Microorganisms, 10 (3), n.spéc. Microbial Non-Ribosomal Synthesis of Secondary Metabolites:577, 19 p.https://doi.org/10.3390/microorganisms10030577 <https://doi.org/10.3390/microorganisms10030577> Nonribosomal peptide synthesis definitely working out of the rules Duban, Matthieu Cociancich, Stéphane Leclère, Valérie eng 2022 Microorganisms F60 - Physiologie et biochimie végétale C30 - Documentation et information peptide synthetase peptide polypeptide biosynthèse métabolite secondaire bioinformatique technique de prévision synthèse bibliographie http://aims.fao.org/aos/agrovoc/c_13231 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_27801 http://aims.fao.org/aos/agrovoc/c_928 http://aims.fao.org/aos/agrovoc/c_34335 http://aims.fao.org/aos/agrovoc/c_37958 http://aims.fao.org/aos/agrovoc/c_3041 http://aims.fao.org/aos/agrovoc/c_3def4163 http://aims.fao.org/aos/agrovoc/c_1335513885866 Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called nonribosomal peptide synthetases. These synthetases are organized in modules constituted of adenylation, thiolation, and condensation core domains. As such, each module governs, according to the collinearity rule, the incorporation of a monomer within the growing peptide. The release of the peptide from the assembly chain is finally performed by a terminal core thioesterase domain. Secondary domains with modifying catalytic activities such as epimerization or methylation are sometimes included in the assembly lines as supplementary domains. This assembly line structure is analyzed by bioinformatics tools to predict the sequence and structure of the final peptides according to the sequence of the corresponding synthetases. However, a constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribosomal peptides. In this review, through several examples, we aim at highlighting these noncanonical pathways in order for the readers to perceive their complexity. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/600447/1/microorganisms-10-00577.pdf text cc_by info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ https://doi.org/10.3390/microorganisms10030577 10.3390/microorganisms10030577 info:eu-repo/semantics/altIdentifier/doi/10.3390/microorganisms10030577 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.3390/microorganisms10030577
institution CIRAD FR
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-cirad-fr
tag biblioteca
region Europa del Oeste
libraryname Biblioteca del CIRAD Francia
language eng
topic F60 - Physiologie et biochimie végétale
C30 - Documentation et information
peptide synthetase
peptide
polypeptide
biosynthèse
métabolite secondaire
bioinformatique
technique de prévision
synthèse
bibliographie
http://aims.fao.org/aos/agrovoc/c_13231
http://aims.fao.org/aos/agrovoc/c_5691
http://aims.fao.org/aos/agrovoc/c_27801
http://aims.fao.org/aos/agrovoc/c_928
http://aims.fao.org/aos/agrovoc/c_34335
http://aims.fao.org/aos/agrovoc/c_37958
http://aims.fao.org/aos/agrovoc/c_3041
http://aims.fao.org/aos/agrovoc/c_3def4163
http://aims.fao.org/aos/agrovoc/c_1335513885866
F60 - Physiologie et biochimie végétale
C30 - Documentation et information
peptide synthetase
peptide
polypeptide
biosynthèse
métabolite secondaire
bioinformatique
technique de prévision
synthèse
bibliographie
http://aims.fao.org/aos/agrovoc/c_13231
http://aims.fao.org/aos/agrovoc/c_5691
http://aims.fao.org/aos/agrovoc/c_27801
http://aims.fao.org/aos/agrovoc/c_928
http://aims.fao.org/aos/agrovoc/c_34335
http://aims.fao.org/aos/agrovoc/c_37958
http://aims.fao.org/aos/agrovoc/c_3041
http://aims.fao.org/aos/agrovoc/c_3def4163
http://aims.fao.org/aos/agrovoc/c_1335513885866
spellingShingle F60 - Physiologie et biochimie végétale
C30 - Documentation et information
peptide synthetase
peptide
polypeptide
biosynthèse
métabolite secondaire
bioinformatique
technique de prévision
synthèse
bibliographie
http://aims.fao.org/aos/agrovoc/c_13231
http://aims.fao.org/aos/agrovoc/c_5691
http://aims.fao.org/aos/agrovoc/c_27801
http://aims.fao.org/aos/agrovoc/c_928
http://aims.fao.org/aos/agrovoc/c_34335
http://aims.fao.org/aos/agrovoc/c_37958
http://aims.fao.org/aos/agrovoc/c_3041
http://aims.fao.org/aos/agrovoc/c_3def4163
http://aims.fao.org/aos/agrovoc/c_1335513885866
F60 - Physiologie et biochimie végétale
C30 - Documentation et information
peptide synthetase
peptide
polypeptide
biosynthèse
métabolite secondaire
bioinformatique
technique de prévision
synthèse
bibliographie
http://aims.fao.org/aos/agrovoc/c_13231
http://aims.fao.org/aos/agrovoc/c_5691
http://aims.fao.org/aos/agrovoc/c_27801
http://aims.fao.org/aos/agrovoc/c_928
http://aims.fao.org/aos/agrovoc/c_34335
http://aims.fao.org/aos/agrovoc/c_37958
http://aims.fao.org/aos/agrovoc/c_3041
http://aims.fao.org/aos/agrovoc/c_3def4163
http://aims.fao.org/aos/agrovoc/c_1335513885866
Duban, Matthieu
Cociancich, Stéphane
Leclère, Valérie
Nonribosomal peptide synthesis definitely working out of the rules
description Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called nonribosomal peptide synthetases. These synthetases are organized in modules constituted of adenylation, thiolation, and condensation core domains. As such, each module governs, according to the collinearity rule, the incorporation of a monomer within the growing peptide. The release of the peptide from the assembly chain is finally performed by a terminal core thioesterase domain. Secondary domains with modifying catalytic activities such as epimerization or methylation are sometimes included in the assembly lines as supplementary domains. This assembly line structure is analyzed by bioinformatics tools to predict the sequence and structure of the final peptides according to the sequence of the corresponding synthetases. However, a constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribosomal peptides. In this review, through several examples, we aim at highlighting these noncanonical pathways in order for the readers to perceive their complexity.
format article
topic_facet F60 - Physiologie et biochimie végétale
C30 - Documentation et information
peptide synthetase
peptide
polypeptide
biosynthèse
métabolite secondaire
bioinformatique
technique de prévision
synthèse
bibliographie
http://aims.fao.org/aos/agrovoc/c_13231
http://aims.fao.org/aos/agrovoc/c_5691
http://aims.fao.org/aos/agrovoc/c_27801
http://aims.fao.org/aos/agrovoc/c_928
http://aims.fao.org/aos/agrovoc/c_34335
http://aims.fao.org/aos/agrovoc/c_37958
http://aims.fao.org/aos/agrovoc/c_3041
http://aims.fao.org/aos/agrovoc/c_3def4163
http://aims.fao.org/aos/agrovoc/c_1335513885866
author Duban, Matthieu
Cociancich, Stéphane
Leclère, Valérie
author_facet Duban, Matthieu
Cociancich, Stéphane
Leclère, Valérie
author_sort Duban, Matthieu
title Nonribosomal peptide synthesis definitely working out of the rules
title_short Nonribosomal peptide synthesis definitely working out of the rules
title_full Nonribosomal peptide synthesis definitely working out of the rules
title_fullStr Nonribosomal peptide synthesis definitely working out of the rules
title_full_unstemmed Nonribosomal peptide synthesis definitely working out of the rules
title_sort nonribosomal peptide synthesis definitely working out of the rules
url http://agritrop.cirad.fr/600447/
http://agritrop.cirad.fr/600447/1/microorganisms-10-00577.pdf
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