Mutations inmut methylmalonic acidemia: Clinical and enzymatic correlations

Human MutationVolume 9, Issue 1 p. 1-6 Mutation Update Mutations in mut methylmalonic acidemia: Clinical and enzymatic correlations Fred D. Ledley, Fred D. Ledley Departments of Cell Biology and Pediatrics, Baylor College of Medicine, Houston, Texas 77030Search for more papers by this authorDavid S. Rosenblatt, Corresponding Author David S. Rosenblatt Medical Research Council of Canada Genetics Group and Departments of Human Genetics, Medicine, Pediatrics, and Biology, McGill University, Montreal, Quebec H3A 1A1; Fax: 617-364-1599Royal Victoria Hospital, 687 Pine Avenue West, H5-63, Montreal Quebec H3A 1A1Search for more papers by this author Fred D. Ledley, Fred D. Ledley Departments of Cell Biology and Pediatrics, Baylor College of Medicine, Houston, Texas 77030Search for more papers by this authorDavid S. Rosenblatt, Corresponding Author David S. Rosenblatt Medical Research Council of Canada Genetics Group and Departments of Human Genetics, Medicine, Pediatrics, and Biology, McGill University, Montreal, Quebec H3A 1A1; Fax: 617-364-1599Royal Victoria Hospital, 687 Pine Avenue West, H5-63, Montreal Quebec H3A 1A1Search for more papers by this author First published: 07 January 1999 https://doi.org/10.1002/(SICI)1098-1004(1997)9:1<1::AID-HUMU1>3.0.CO;2-ECitations: 45AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract 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 muto 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 muto 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. Citing Literature Volume9, Issue11997Pages 1-6 RelatedInformation