ArticleThe Journal of biological chemistry2020
d-Alanine-d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
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- Metabolic Profiles of Clinical Isolates of Drug-Susceptible and Multidrug-ResistantInfection and drug resistance · 2023Article
- Biosynthesis and characterization of fuscimiditide, an aspartimidylated graspetide.Nature chemistry · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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