Hereditary disorders of enzymes in the Embden-Meyerhof pathway of glycolysis.
Recent advances in hereditary disorders of red cell enzymes in the Embden-Meyerhof pathway and the Rapoport-Luebering cycle are discussed with a stress on pyruvate kinase deficiency. Broad genetic heterogeneity exists in all the known erythroenzymopathies. The primary structure of normal human red cell phosphoglycerate kinase has been determined recently and single amino acid substitutions of four mutant phosphoglycerate kinases have been clarified. These studies allowed an analysis of the structure-function relationships at the molecular level more precisely than has been possible previously. It is the consensus of the investigators working in this field that the pathogenesis in three-quarters of the congenital nonspherocytic hemolytic anemia patients remains unknown even after adequate red cell enzyme studies and isopropanol test. This means that broad studies have to be carried out in this field.
D000746:Anemia, Hemolytic, Congenital Nonspherocytic; D001731:Bisphosphoglycerate Mutase / Q000172:deficiency; D005634:Fructose-Bisphosphate Aldolase / Q000172:deficiency; D006019:Glycolysis; D006593:Hexokinase / Q000172:deficiency; D006801:Humans; D008661:Metabolism, Inborn Errors / Q000378:metabolism*; D010732:Phosphofructokinase-1 / Q000172:deficiency; D010735:Phosphoglycerate Kinase / Q000172:deficiency; D011770:Pyruvate Kinase / Q000172:deficiency; D014305:Triose-Phosphate Isomerase / Q000172:deficiency
D006593:Hexokinase; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D010735:Phosphoglycerate Kinase; D005634:Fructose-Bisphosphate Aldolase; D014305:Triose-Phosphate Isomerase; D001731:Bisphosphoglycerate Mutase