Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase

Jimin Gao, Lewis Waber, Michael J. Bennett, K. Michael Gibson, Jonathan C. Cohen

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


Malonyl coenzyme A (CoA) decarboxylase (E.C.4. 1.1.9) catalyzes the conversion of malonyl CoA to acetyl CoA. The metabolic role of malonyl CoA decarboxylase has not been fully defined, but deficiency of the enzyme has been associated with mild mental retardation, seizures, hypotonia, cardiomyopathy, vomiting, hypoglycemia, metabolic acidosis, and malonic aciduria. Here we report the isolation and sequencing of the human gene encoding malonyl CoA decarboxylase, and the identification of a mutation causing malonyl CoA decarboxylase deficiency. Human malonyl CoA decarboxylase cDNA sequences were identified by homology to the goose gene, and the intron/exon boundaries were determined by direct sequencing of a PAC clone containing the entire human gene. The 1479 basepair human cDNA is 70 percent identical to the goose sequence, and the intron/exon boundaries are completely conserved between the two species. The genetic mutation underlying malonyl CoA decarboxylase deficiency was determined in a patient with clinical features of this defect, malonic aciduria, and markedly reduced malonyl CoA decarboxylase activity.

Original languageEnglish (US)
Pages (from-to)178-182
Number of pages5
JournalJournal of lipid research
Issue number1
StatePublished - Jan 1999


  • Frameshift mutation
  • Inborn errors
  • Metabolism
  • Microbodies
  • Mitochondria

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology


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