title: Red cell glycolytic enzyme disorders caused by mutations: an update.
abstract: Glycolysis is one of the principle pathways of ATP generation in cells and is present in all cell tissues; in erythrocytes, glycolysis is the only pathway for ATP synthesis since mature red cells lack the internal structures necessary to produce the energy vital for life. Red cell deficiencies have been detected in all erythrocyte glycolytic pathways, although their frequencies differ owing to diverse causes, such as the affected enzyme and severity of clinical manifestations. The number of enzyme deficiencies known is endless. The most frequent glycolysis abnormality is pyruvate kinase deficiency, since around 500 cases are known, the first of which was reported in 1961. However, only approximately 200 cases were due to mutations. In contrast, only one case of phosphoglycerate mutase BB type mutation, described in 2003, has been detected. Most mutations are located in the coding sequences of genes, while others, missense, deletions, insertions, splice defects, premature stop codons and promoter mutations, are also frequent. Understanding of the crystal structure of enzymes permits molecular modelling studies which, in turn, reveal how mutations can affect enzyme structure and function.
authors.affiliation: Departament de Ciències Fisiològiques I, Unitat de Bioquímica, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Facultat de Medicina, Universitat de Barcelona, Casanova 143, 08036 Barcelona, Spain. fcliment@ub.edu
authors.forename: Fernando
authors.initials: F
authors.lastname: Climent
authors.forename: Feliu
authors.initials: F
authors.lastname: Roset
authors.forename: Ada
authors.initials: A
authors.lastname: Repiso
authors.forename: Pablo
authors.initials: P
authors.lastname: Pérez de la Ossa
mesh_terms: D000743:Anemia, Hemolytic / Q000201:enzymology / Q000235:genetics; D000746:Anemia, Hemolytic, Congenital Nonspherocytic; D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000172:deficiency / Q000235:genetics; D004912:Erythrocytes / Q000201:enzymology; D005956:Glucose-6-Phosphate Isomerase / Q000235:genetics; D006019:Glycolysis; D006801:Humans; D007535:Isomerases / Q000172:deficiency / Q000235:genetics*; D009154:Mutation; D010735:Phosphoglycerate Kinase / Q000172:deficiency / Q000235:genetics; D010736:Phosphoglycerate Mutase / Q000172:deficiency / Q000235:genetics; D011770:Pyruvate Kinase / Q000172:deficiency / Q000235:genetics; D014166:Transferases / Q000172:deficiency / Q000235:genetics*; D014305:Triose-Phosphate Isomerase / Q000172:deficiency / Q000235:genetics
chemical_list: D014166:Transferases; D011770:Pyruvate Kinase; D010735:Phosphoglycerate Kinase; D007535:Isomerases; D014305:Triose-Phosphate Isomerase; D005956:Glucose-6-Phosphate Isomerase; D010736:Phosphoglycerate Mutase; D001731:Bisphosphoglycerate Mutase