Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes

Phosphoglycerate kinase (PGK) deficiency is generally asso-ciated with chronic hemolytic anemia, although it can be accompanied by either mental retardation or muscular dis-ease. Genomic DNAs of two PGK-deficient patients pre-viously described in France were sequenced directly after polymerase chain reaction amplification. The PGK Creteil variant arises from a G-t A nucleotide interchange at posi-tion 1022 in cDNA (exon 9). resulting in amino acid substitu-tion 314 Asp--t Asn in the C-terminal domain, which contains the nucleotide binding site. lt is associeted with rhabdomyo-lysis crises but not with hemolysis or mental retardation. In HOSPHOGLYCERATE KINASE (adenosine triphos-phate [ATP] 3-phosphoglycerate l-phosphotransferase, EC 2.7.2.3: PGK) is a glycolytic enzyme catalyzing the con-version of 1,3-diphosphoglycerate to 3-phosphoglycerat