LD-transpeptidases: the great unknown among the peptidoglycan cross-linkers.
D-amino acids
LD-transpeptidase
cross-linking
peptidoglycan
stress
β-lactams
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
revised:
05
05
2021
received:
20
02
2021
accepted:
09
06
2021
pubmed:
11
6
2021
medline:
19
8
2022
entrez:
10
6
2021
Statut:
ppublish
Résumé
The peptidoglycan (PG) cell wall is an essential polymer for the shape and viability of bacteria. Its protective role is in great part provided by its mesh-like character. Therefore, PG-cross-linking enzymes like the penicillin-binding proteins (PBPs) are among the best targets for antibiotics. However, while PBPs have been in the spotlight for more than 50 years, another class of PG-cross-linking enzymes called LD-transpeptidases (LDTs) seemed to contribute less to PG synthesis and, thus, has kept an aura of mystery. In the last years, a number of studies have associated LDTs with cell wall adaptation to stress including β-lactam antibiotics, outer membrane stability, and toxin delivery, which has shed light onto the biological meaning of these proteins. Furthermore, as some species display a great abundance of LD-cross-links in their cell wall, it has been hypothesized that LDTs could also be the main synthetic PG-transpeptidases in some bacteria. In this review, we introduce these enzymes and their role in PG biosynthesis and we highlight the most recent advances in understanding their biological role in diverse species.
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Proteins
0
Penicillin-Binding Proteins
0
Peptidoglycan
0
Peptidyl Transferases
EC 2.3.2.12
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4718-4730Informations de copyright
© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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