The novel mutation p.Asp251Asn in the β-subunit of succinate-CoA ligase causes encephalomyopathy and elevated succinylcarnitine
| Autor: | Brandy Klotzle, Elham Jaberi, Masoud Houshmand, Elahe Elahi, Mohammad Rohani, Iman Safari, Maryam Malakouti Nejad, Farzad Sina, Fereshteh Chitsazian, Gholam Ali Shahidi |
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| Rok vydání: | 2012 |
| Předmět: |
Adult
Male Mitochondrial DNA SUCLA2 Methylmalonic acid chemistry.chemical_compound Mitochondrial Encephalomyopathies Carnitine Succinate-CoA Ligases Genetics Humans Child Gene Genetics (clinical) chemistry.chemical_classification ATP synthase biology Infant Newborn Brain Infant Molecular biology Magnetic Resonance Imaging Amino acid Pedigree Enzyme chemistry Biochemistry Amino Acid Substitution Child Preschool Mutation biology.protein Female |
| Zdroj: | Journal of human genetics. 58(8) |
| ISSN: | 1435-232X |
| Popis: | SUCLA2 is one of several nuclear-encoded genes that can cause encephalomyopathy accompanied by mitochondrial DNA depletion. The disorder usually manifests in early childhood and leads to early death. The gene encodes one of the subunits of succinyl-CoA synthase, the enzyme that catalyzes the reversible conversion of substrates succinyl-CoA and ADP to products succinate and ATP in the tricarboxylic acid pathway. Thirty-two individuals harboring mutations in SUCLA2 have so far been reported, and five different mutations were observed among these individuals. Here we report identification of a novel mutation in SUCLA2 in two cousins affected with encephalomyopathy. The novel mutation causes p.Asp251Asn; the affected amino acid is likely positioned within the ATP-grasp domain of the encoded protein. As previously reported in other patients, we did not observe elevation of methylmalonic acid, the biochemical hallmark of patients with mutations in SUCLA2. We instead found elevated levels of succinylcarnitine. |
| Databáze: | OpenAIRE |
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