ArticleBMC biochemistry2002
The Caenorhabditis elegans Y87G2A.14 Nudix hydrolase is a peroxisomal coenzyme A diphosphatase.
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 15 papers.
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15 citing papers in PubMed, 26 citations in OpenAlex.
- Turnover rate of coenzyme A in mouse brain and liver.PloS one · 2021Article
- Regulation of coenzyme A levels by degradation: the 'Ins and Outs'.Progress in lipid research · 2020Review
- Article
- Plant peroxisomal solute transporter proteins.Journal of integrative plant biology · 2019Review
- Nudt8 is a novel CoA diphosphohydrolase that resides in the mitochondria.FEBS letters · 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
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- Extracellular 4'-phosphopantetheine is a source for intracellular coenzyme A synthesis.Nature chemical biology · 2015Article
- Molecular identification of Trichinella spiralis nudix hydrolase and its induced protective immunity against trichinellosis in BALB/c mice.Parasites & vectors · 2014Article
- Molecular characterization of organelle-type Nudix hydrolases in Arabidopsis.Plant physiology · 2008Article
- Identification of functional domains in Arabidopsis thaliana mRNA decapping enzyme (AtDcp2).Nucleic acids research · 2008Article
- Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity.The Biochemical journal · 2006Article
- Characterization of a nudix hydrolase from Deinococcus radiodurans with a marked specificity for (deoxy)ribonucleoside 5'-diphosphates.BMC biochemistry · 2004Article
- Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein.The Biochemical journal · 2003Article
- Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family.Journal of bacteriology · 2003Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe number of Nudix hydrolase family members varies widely among different organisms. In order to understand the reasons for the particular spectrum possessed by a given organism, the substrate specificity and function of different family members must be established.
resultsThe Y87G2A.14 Nudix hydrolase gene product of Caenorhabditis elegans has been expressed as a thioredoxin fusion protein in Escherichia coli and shown to be a CoA diphosphatase with catalytic activity towards CoA and its derivatives. The products of CoA hydrolysis were 3',5'-ADP and 4'-phosphopantetheine with Km and kcat values of 220 microM and 13.8 s(-1) respectively. CoA esters yielded 3',5'-ADP and the corresponding acyl-phosphopantetheine. Activity was optimal at pH 9.5 with 5 mM Mg2+ and fluoride was inhibitory with a Ki of 3 microM. The Y87G2A.14 gene product has a potential C-terminal tripeptide PTS1 peroxisomal targeting signal - SKI. By fusing a Y87G2A.14 cDNA to the C-terminus of yeast-enhanced green fluorescent protein, the enzyme appeared to be targeted to peroxisomes by the SKI signal when transfected into yeast cells. Deletion of SKI abolished specific targeting.
conclusionsThe presence of related sequences with potential PTS1 or PTS2 peroxisomal targeting signals in other organisms suggests a conserved peroxisomal function for the CoA diphosphatase members of this group of Nudix hydrolases.
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