Molecular and structural analysis of two novel mutations in a patient with mut(-) methylmalonyl-CoA deficiency

Mol Genet Metab. 2001 Feb;72(2):181-4. doi: 10.1006/mgme.2000.3122.

Abstract

Inherited defects in the gene encoding the methylmalonyl-CoA mutase (MCM) result in the mut forms of methylmalonic aciduria (MMA). Twelve mutations have been identified associated with the mut(-) phenotype. We report two novel mutations (K621N and D156N) in a compound heterozygote mut(-) patient. These two mutations and three previously published ones (H627N, A191E, Y231N) were mapped onto a three-dimensional homology model of the human MCM constructed from the crystal structure of the Propionibacterium shermanii enzyme.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / chemistry*
  • Acyl Coenzyme A / deficiency*
  • Acyl Coenzyme A / genetics*
  • Child, Preschool
  • Female
  • Genotype
  • Heterozygote
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Mutation*
  • Mutation, Missense*
  • Phenotype
  • Propionibacterium / enzymology
  • Protein Structure, Tertiary

Substances

  • Acyl Coenzyme A
  • methylmalonyl-coenzyme A

Associated data

  • OMIM/251000