ArticleJournal of bacteriology2003
Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Fatty acid composition and gene regulatory network analysis of pectoral muscle in pigeons across developmental stages.Food chemistry. Molecular sciences · 2025Article
- Molecular Dialogues between Early Divergent Fungi and Bacteria in an Antagonism versus a Mutualism.mBio · 2020Article
- Regulation of coenzyme A levels by degradation: the 'Ins and Outs'.Progress in lipid research · 2020Review
- A cryptic activity in the Nudix hydrolase superfamily.Protein science : a publication of the Protein Society · 2019Article
- Structural analyses of NudT16-ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins.Scientific reports · 2019Article
- Nudt19 is a renal CoA diphosphohydrolase with biochemical and regulatory properties that are distinct from the hepatic Nudt7 isoform.The Journal of biological chemistry · 2018Article
- Nudix hydrolases degrade protein-conjugated ADP-ribose.Scientific reports · 2015Article
- Structural and Enzymatic Characterization of a Nucleoside Diphosphate Sugar Hydrolase from Bdellovibrio bacteriovorus.PloS one · 2015Article
- Structural and functional insights into DR2231 protein, the MazG-like nucleoside triphosphate pyrophosphohydrolase from Deinococcus radiodurans.The Journal of biological chemistry · 2011Article
- Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base.The Journal of biological chemistry · 2010Article
- Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Structure and biological function of the RNA pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus.Structure (London, England : 1993) · 2009Article
- Four enzymes define the incorporation of coenzyme A in thienamycin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Article
- Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites.Cell cycle (Georgetown, Tex.) · 2008Article
- Overexpression, crystallization and preliminary X-ray crystallographic analysis of Nudix hydrolase Orf141 from Escherichia coli K-1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Biosynthesis of Pantothenic Acid and Coenzyme A.EcoSal Plus · 2007Article
- Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis.Journal of bacteriology · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Gene Dr1184 from Deinococcus radiodurans codes for a Nudix enzyme (DR-CoAse) that hydrolyzes the pyrophosphate moiety of coenzyme A (CoA). Nudix enzymes with the same specificity have been found in yeast, humans, and mice. The three-dimensional structure of DR-CoAse, the first of a Nudix hydrolase with this specificity, reveals that this enzyme contains, in addition to the fold observed in other Nudix enzymes, insertions that are characteristic of a CoA-hydrolyzing Nudix subfamily. The structure of the complex of the enzyme with Mg(2+), its activating cation, reveals the position of the catalytic site. A helix, part of the N-terminal insertion, partially occludes the binding site and has to change its position to permit substrate binding. Comparison of the structure of DR-CoAse to those of other Nudix enzymes, together with the location in the structure of the sequence characteristic of CoAses, suggests a mode of binding of the substrate to the enzyme that is compatible with all available data.
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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.