A novel SUCLA2 mutation in a Portuguese child associated with "mild" methylmalonic Aciduria

Célia Nogueira, Maria Chiara Meschini, Claudia Nesti, Paula Garcia, Luisa Diogo, Carla Valongo, Ricardo Costa, Arnaldo Videira, Laura Vilarinho, Filippo M. Santorelli

Research output: Contribution to journalArticlepeer-review


Succinyl-coenzyme A synthase is a mitochondrial matrix enzyme that catalyzes the reversible synthesis of succinate and adenosine triphosphate (ATP) from succinyl-coenzyme A and adenosine diphosphate (ADP) in the tricarboxylic acid cycle. This enzyme is made up of a and b subunits encoded by SUCLG1 and SUCLA2, respectively. We present a child with severe muscular hypotonia, dystonia, failure to thrive, sensorineural deafness, and dysmorphism. Metabolic investigations disclosed hyperlactacidemia, moderate urinary excretion of methylmalonic acid, and elevated levels of C4-dicarboxylic carnitine in blood. We identified a novel homozygous p.M329V in SUCLA2. In cultured cells, the p.M329V resulted in a reduced amount of the SUCLA2 protein, impaired production of mitochondrial ATP, and enhanced production of reactive oxygen species, which was partially reduced by using 5-aminoimidazole-4-carboxamide ribonucleotide in the culture medium. Expanding the array of SUCLA2 mutations, we suggested that reactive oxygen species scavengers are likely to impact on disease prognosis.

Original languageEnglish
Pages (from-to)228-232
Number of pages5
JournalJournal of Child Neurology
Issue number2
Publication statusPublished - 2015


  • Encephalomyopathy
  • Methylmalonic aciduria
  • Mitochondrial DNA depletion
  • Succinate-coenzyme A ligase
  • SUCLA2

ASJC Scopus subject areas

  • Clinical Neurology
  • Pediatrics, Perinatology, and Child Health
  • Medicine(all)


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