The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency.
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).[1]References
- The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency. Tsujino, S., Shanske, S., Sakoda, S., Fenichel, G., DiMauro, S. Am. J. Hum. Genet. (1993) [Pubmed]
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