ArticleBMC biochemistry2002
Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases.
Article in BMC biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
- Optimization of a high throughput screening platform to identify inhibitors of asymmetric diadenosine polyphosphatases.Analytical biochemistry · 2025Article
- Expression and Potential Biomarkers of Regulators for M7G RNA Modification in Gliomas.Frontiers in neurology · 2022Article
- New structural insights reveal an expanded reaction cycle for inositol pyrophosphate hydrolysis by human DIPP1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- InsPProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Prodigal Compound: Return of Ribosyl 1,5-Bisphosphate as an Important Player in Metabolism.Microbiology and molecular biology reviews : MMBR · 2019Review
- Article
- The inositol pyrophosphate pathway in health and diseases.Biological reviews of the Cambridge Philosophical Society · 2018Review
- A comprehensive structural, biochemical and biological profiling of the human NUDIX hydrolase family.Nature communications · 2017Article
- Structural and Enzymatic Characterization of a Nucleoside Diphosphate Sugar Hydrolase from Bdellovibrio bacteriovorus.PloS one · 2015Article
- Article
- The enzymes of human diphosphoinositol polyphosphate metabolism.The FEBS journal · 2014Review
- Understanding inositol pyrophosphate metabolism and function: kinetic characterization of the DIPPs.FEBS letters · 2013Article
- Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?Cellular and molecular life sciences : CMLS · 2013Article
- Structural insight into inositol pyrophosphate turnover.Advances in biological regulation · 2013Review
- Diphosphoinositol polyphosphates: what are the mechanisms?Advances in enzyme regulation · 2011Review
- Inositol pyrophosphates: structure, enzymology and function.Cellular and molecular life sciences : CMLS · 2009Review
- Diphosphoinositol polyphosphates: metabolic messengers?Molecular pharmacology · 2009Review
- Sexy gene conversions: locating gene conversions on the X-chromosome.Nucleic acids research · 2009Article
- Characterization of a nudix hydrolase from Deinococcus radiodurans with a marked specificity for (deoxy)ribonucleoside 5'-diphosphates.BMC biochemistry · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe human genome contains at least 18 genes for Nudix hydrolase enzymes. Many have similar functions to one another. In order to understand their roles in cell physiology, these proteins must be characterised.
resultsWe have characterised two novel human gene products, hAps1, encoded by the NUDT11 gene, and hAps2, encoded by the NUDT10 gene. These cytoplasmic proteins are members of the DIPP subfamily of Nudix hydrolases, and differ from each other by a single amino acid. Both metabolise diadenosine-polyphosphates and, weakly, diphosphoinositol polyphosphates. An apparent polymorphism of hAps1 has also been identified, which leads to the point mutation S39N. This has also been characterised. The favoured nucleotides were diadenosine 5',5"'-pentaphosphate (kcat/Km = 11, 8 and 16 x 10(3) M(-1) x s(-1) respectively for hAps1, hAps1-39N and hAps2) and diadenosine 5',5"'-hexaphosphate (kcat/Km = 13, 14 and 11 x 10(3) M(-1) x s(-1) respectively for hAps1, hAps1-39N and hAps2). Both hAps1 and hAps2 had pH optima of 8.5 and an absolute requirement for divalent cations, with manganese (II) being favoured. Magnesium was not able to activate the enzymes. Therefore, these enzymes could be acutely regulated by manganese fluxes within the cell.
conclusionsRecent gene duplication has generated the two Nudix genes, NUDT11 and NUDT10. We have characterised their gene products as the closely related Nudix hydrolases, hAps1 and hAps2. These two gene products complement the activity of previously described members of the DIPP family, and reinforce the concept that Ap5A and Ap6A act as intracellular messengers.
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