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Molecular and structural analysis of two novel mutations in a patient with mut(-) methylmalonyl-CoA deficiency
J F Benoist1, C Acquaviva, I Callebaut
1Service de Biochimie-Hormonologie, Assitanace Publique-Hôpitaux de Paris, Hôpital Robert Debré, 48 Bd Sérurier, 75019 Paris, France. jean-francois.benoist@rdb.ap-hop-paris.fr
Molecular Genetics and Metabolism
|February 13, 2001
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.