ArticleBiochemical and biophysical research communications2013
Crystal structure of wild-type and mutant human Ap4A hydrolase.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 13 citations in OpenAlex.
- Optimization of a high throughput screening platform to identify inhibitors of asymmetric diadenosine polyphosphatases.Analytical biochemistry · 2025Article
- Biallelic NUDT2 variants defective in mRNA decapping cause a neurodevelopmental disease.Brain : a journal of neurology · 2024Article
- Template-Based Modelling of the Structure of Fungal Effector Proteins.Molecular biotechnology · 2024Article
- Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate byBiochemistry · 2023Article
- NUDT2 initiates viral RNA degradation by removal of 5'-phosphates.Nature communications · 2021Article
- Article
- Global profiling of lysine reactivity and ligandability in the human proteome.Nature chemistry · 2017Article
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- Structural and functional attributes of malaria parasite diadenosine tetraphosphate hydrolase.Scientific reports · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ap4A hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human Ap4A hydrolase. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common αβα-sandwich architecture. Interestingly, two sulfate ions and one diphosphate coordinated with some conserved residues were observed in the active cleft, which affords a better understanding of a possible mode of substrate binding.
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