coenzyme-q10 and pyrimidine

coenzyme-q10 has been researched along with pyrimidine* in 2 studies

Other Studies

2 other study(ies) available for coenzyme-q10 and pyrimidine

Article	Year
Bypassing human CoQ Molecular genetics and metabolism, 2018, Volume: 123, Issue:3 Primary disorders of the human coenzyme Q Topics: Animals; Apoptosis; Ataxia; Biosynthetic Pathways; Cytochrome P-450 Enzyme System; Disease Models, Animal; Humans; Hydroxybenzoates; Mice; Mitochondria; Mitochondrial Diseases; Muscle Weakness; Pyrimidines; Solubility; Treatment Outcome; Ubiquinone; Vitamins	2018
Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis. Human molecular genetics, 2007, May-01, Volume: 16, Issue:9 Coenzyme Q(10) (CoQ(10)) deficiency has been associated with an increasing number of clinical phenotypes that respond to CoQ(10) supplementation. In two siblings with encephalomyopathy, nephropathy and severe CoQ(10) deficiency, a homozygous mutation was identified in the CoQ(10) biosynthesis gene COQ2, encoding polyprenyl-pHB transferase. To confirm the pathogenicity of this mutation, we have demonstrated that human wild-type, but not mutant COQ2, functionally complements COQ2 defective yeast. In addition, an equivalent mutation introduced in the yeast COQ2 gene also decreases both CoQ(6) concentration and growth in respiratory-chain dependent medium. Polyprenyl-pHB transferase activity was 33-45% of controls in COQ2 mutant fibroblasts. CoQ-dependent mitochondrial complexes activities were restored in deficient fibroblasts by CoQ(10) supplementation, and growth rate was restored in these cells by either CoQ(10) or uridine supplementation. This work is the first direct demonstration of the pathogenicity of a COQ2 mutation involved in human disease, and establishes yeast as a useful model to study human CoQ(10) deficiency. Moreover, we demonstrate that CoQ(10) deficiency in addition to the bioenergetics defect also impairs de novo pyrimidine synthesis, which may contribute to the pathogenesis of the disease. Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Base Sequence; Cell Division; Cells, Cultured; Coenzymes; Energy Metabolism; Enzyme Activation; Fibroblasts; Genetic Complementation Test; HeLa Cells; Humans; Immunoblotting; Mitochondria; Molecular Sequence Data; Mutation, Missense; Prohibitins; Pyrimidines; Saccharomyces cerevisiae; Sequence Alignment; Ubiquinone; Uridine	2007

Article

Year

Molecular genetics and metabolism, 2018, Volume: 123, Issue:3

Primary disorders of the human coenzyme Q

Topics: Animals; Apoptosis; Ataxia; Biosynthetic Pathways; Cytochrome P-450 Enzyme System; Disease Models, Animal; Humans; Hydroxybenzoates; Mice; Mitochondria; Mitochondrial Diseases; Muscle Weakness; Pyrimidines; Solubility; Treatment Outcome; Ubiquinone; Vitamins

2018

Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis.

Human molecular genetics, 2007, May-01, Volume: 16, Issue:9

Coenzyme Q(10) (CoQ(10)) deficiency has been associated with an increasing number of clinical phenotypes that respond to CoQ(10) supplementation. In two siblings with encephalomyopathy, nephropathy and severe CoQ(10) deficiency, a homozygous mutation was identified in the CoQ(10) biosynthesis gene COQ2, encoding polyprenyl-pHB transferase. To confirm the pathogenicity of this mutation, we have demonstrated that human wild-type, but not mutant COQ2, functionally complements COQ2 defective yeast. In addition, an equivalent mutation introduced in the yeast COQ2 gene also decreases both CoQ(6) concentration and growth in respiratory-chain dependent medium. Polyprenyl-pHB transferase activity was 33-45% of controls in COQ2 mutant fibroblasts. CoQ-dependent mitochondrial complexes activities were restored in deficient fibroblasts by CoQ(10) supplementation, and growth rate was restored in these cells by either CoQ(10) or uridine supplementation. This work is the first direct demonstration of the pathogenicity of a COQ2 mutation involved in human disease, and establishes yeast as a useful model to study human CoQ(10) deficiency. Moreover, we demonstrate that CoQ(10) deficiency in addition to the bioenergetics defect also impairs de novo pyrimidine synthesis, which may contribute to the pathogenesis of the disease.

Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Base Sequence; Cell Division; Cells, Cultured; Coenzymes; Energy Metabolism; Enzyme Activation; Fibroblasts; Genetic Complementation Test; HeLa Cells; Humans; Immunoblotting; Mitochondria; Molecular Sequence Data; Mutation, Missense; Prohibitins; Pyrimidines; Saccharomyces cerevisiae; Sequence Alignment; Ubiquinone; Uridine

2007