ReviewBioorganic chemistry2011
The ATP-grasp enzymes.
Review in Bioorganic chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
106 citing papers in PubMed, 183 citations in OpenAlex.
- Late-Stage Posttranslational Assembly of Fosfazinomycins.bioRxiv : the preprint server for biology · 2026Article
- Catalytic loop closure governs substrate selectivity in the rhizocticin biosynthetic ligases RhiM and RhiC.The Journal of biological chemistry · 2026Article
- A posttranslational modification of fimbriae drives pathogenicity inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Nature Counts to Three: Universal Mg-Pinch Motif Polarizes the Cleaved Bond in NTP-Processing Enzymes.Journal of the American Chemical Society · 2026Article
- The evolution of gene functional repertoire in Amorphea: divergent strategies across Amoebozoa, Fungi, and Metazoa.Molecular biology and evolution · 2026Article
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A platform for CRISPRi-seq inmBio · 2026Article
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Enzymatic combinatorial synthesis of E-64 and related cysteine protease inhibitors.Nature chemical biology · 2025Article
- A novel post-translational modification of fimbriae drives pathogenicity inbioRxiv : the preprint server for biology · 2025Article
- Identification and characterization of archaeal pseudomurein biosynthesis genes through pangenomics.mSystems · 2025Article
- Blasticidin S Biosynthesis Involves a Unique Interplay between a Radical SAM Dehydratase, a Transaminase and an ATP-Grasp Ligase in Order to Avoid a Futile Cycle.ACS catalysis · 2025Article
- Structural basis of Spliced Leader RNA recognition by the Trypanosoma brucei cap-binding complex.Nature communications · 2025Article
- Bioinformatics study of biotin carboxylase B-subdomain isolated fromBiotechnologia · 2025Article
- Inositol Phosphate Kinase Architecture: Practical Approaches and Lessons Learned.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Characterization of a Dual Function Peptide Cyclase in Graspetide Biosynthesis.ACS chemical biology · 2024Article
- Discovery, functional characterization, and structural studies of the NRPS-independent siderophore synthetases.Critical reviews in biochemistry and molecular biology · 2024Review
- Mining Translation Inhibitors by a Unique Peptidyl-Aminonucleoside Synthetase Reveals Cystocin Biosynthesis and Self-Resistance.International journal of molecular sciences · 2024Article
- Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The ATP-grasp enzymes consist of a superfamily of 21 proteins that contain an atypical ATP-binding site, called the ATP-grasp fold. The ATP-grasp fold is comprised of two α+β domains that "grasp" a molecule of ATP between them and members of the family typically have an overall structural design containing three common conserved focal domains. The founding members of the family consist of biotin carboxylase, d-ala-d-ala ligase and glutathione synthetase, all of which catalyze the ATP-assisted reaction of a carboxylic acid with a nucleophile via the formation of an acylphosphate intermediate. While most members of the superfamily follow this mechanistic pathway, studies have demonstrated that two enzymes catalyze only the phosphoryl transfer step and thus are kinases instead of ligases. Members of the ATP-grasp superfamily are found in several metabolic pathways including de novo purine biosynthesis, gluconeogenesis, and fatty acid synthesis. Given the critical nature of these enzymes, researchers have actively sought the development of potent inhibitors of several members of the superfamily as antibacterial and anti-obseity agents. In this review, we will discuss the structure, function, mechanism, and inhibition of the ATP-grasp enzymes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.