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Seven novel mutations in mut methylmalonic aciduria

โœ Scribed by Charles E. Adjalla; Angela R. Hosack; Brian M. Gilfix; Estelle Lamothe; Sophie Sun; Adrian Chan; Stacey Evans; Nora V. Matiaszuk; David S. Rosenblatt

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
140 KB
Volume
11
Category
Article
ISSN
1059-7794

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โœฆ Synopsis

Methylmalonic aciduria (MMA) is an autosomal recessive inborn error of metabolism that results from functional defects in methylmalonyl CoA mutase (MCM), a nuclear-encoded, mitochondrial enzyme that uses the vitamin B 12 derivative, adenosylcobalamin (AdoCbl) as a cofactor. To date, 23 mutations have been identified at the MUT locus on the short arm of chromosome 6, causing the mut forms of MMA (mut complementation group; mut MMA, McKusick #251000). We now report seven novel mutations. Three were found in mut 0 patients: R228Q (c759GยฎA) was found as a heterozygous change; G312V (c1011GยฎT) and 346delL (c1112delCTT) were both found as homozygous changes. Four mutations were found in mut -patients: A191E (c648CยฎA) and V633G (c1974TยฎG) were found in the same patient; 684insL (c2128insCTC) and L685R (c2130TยฎG) were both found as homozygous changes. The recent modelling of the human methylmalonyl CoA mutase allowed for an interpretation of the identified mutations.

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