d-Alanine-d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations.
ATP-grasp
X-ray crystallography
d-alanine–d-alanine ligase (Ddl)
enzyme catalysis
enzyme kinetics
enzyme mechanism
enzyme structure
metal activation
metal ion–protein interaction
monovalent cation
structural biology
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
05 06 2020
05 06 2020
Historique:
received:
05
02
2020
revised:
23
04
2020
pubmed:
27
4
2020
medline:
29
12
2020
entrez:
27
4
2020
Statut:
ppublish
Résumé
The ATP-grasp superfamily of enzymes shares an atypical nucleotide-binding site known as the ATP-grasp fold. These enzymes are involved in many biological pathways in all domains of life. One ATP-grasp enzyme, d-alanine-d-alanine ligase (Ddl), catalyzes ATP-dependent formation of the d-alanyl-d-alanine dipeptide essential for bacterial cell wall biosynthesis and is therefore an important antibiotic drug target. Ddl is activated by the monovalent cation (MVC) K
Identifiants
pubmed: 32335509
pii: S0021-9258(17)49431-2
doi: 10.1074/jbc.RA120.012936
pmc: PMC7278361
doi:
Substances chimiques
Cations, Monovalent
0
Metals, Alkali
0
Adenosine Triphosphate
8L70Q75FXE
Peptide Synthases
EC 6.3.2.-
D-alanylalanine synthetase
EC 6.3.2.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7894-7904Informations de copyright
© 2020 Pederick et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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