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Mutations in mut methylmalonic acidemia: Clinical and enzymatic correlations
Author(s) -
Ledley Fred D.,
Rosenblatt David S.
Publication year - 1997
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/(sici)1098-1004(1997)9:1<1::aid-humu1>3.0.co;2-e
Subject(s) - methylmalonic acidemia , biology , mutase , genetics , complementation , phenotype , gene , enzyme , biochemistry , endocrinology
Mut methylmalonic acidemia is caused by mutations in the MUT locus encoding the enzyme methylmalonyl CoA mutase. Genotypic and phenotypic variability in this disease has been studied extensively by biochemical and somatic cell genetic techniques, by molecular cloning, and by gene transfer. Mutations have been identified that cause classic mut o phenotypes in which there is no detectable enzymatic activity, mut − phenotypes in which there is residual cobalamin‐dependent activity, as well as a subset within both mut o and mut − phenotypes that exhibit interallelic complementation. These mutations illustrate the position, structure, and function of critical domains within this cobalamin‐binding enzyme and provide new insights into the biochemical and clinical consequences of enzyme deficiency. © 1997 Wiley‐Liss, Inc.