The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency.

Authors: Tsujino, S  Shanske, S  Sakoda, S  Fenichel, G  DiMauro, S 
Citation: Tsujino S, etal., Am J Hum Genet. 1993 Mar;52(3):472-7.
Pubmed: (View Article at PubMed) PMID:8447317

The glycolytic enzyme phosphoglycerate mutase (PGAM) is a dimer, and mature human skeletal muscle contains almost exclusively the MM form of the enzyme, PGAM-M. In 1981, we identified a patient with PGAM-M deficiency, and three additional patients have since been described. All presented with exercise intolerance, cramps, and myoglobinuria. We report two new patients with PGAM-M deficiency and describe the molecular lesions in five patients--four African-Americans and one Caucasian. Three patients were homozygous for an identical G-to-A transition converting an encoded Trp to an in-frame stop codon (codon 78). A fourth patient was heterozygous for this mutation and also carried an A-to-C mutation converting Glu to Ala (codon 89). The fifth patient, the only Caucasian, was homozygous for a different point mutation, a C-to-T mutation, converting Arg to Trp (codon 90).

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RGD ID: 1599129
Created: 2007-01-17
Species: All species
Last Modified: 2007-01-17
Status: ACTIVE