Open AccessGlucose‐6‐phosphate dehydrogenase
Author(s) -
JEFFERY Jonathan,
BARROSSÖDERLING Jane,
MURRAY Lynda,
WOOD Irene,
HANSEN Robert,
SZEPESI Bela,
JÖRNVALL Hans
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb15242.x
Subject(s) - dehydrogenase , enzyme , biology , opossum , biochemistry , glucose 6 phosphate dehydrogenase , protein primary structure , amino acid , mutant , phosphate , marsupial , homologous chromosome , peptide sequence , gene , anatomy , ecology
The primary structure of glucose‐6‐phosphate dehydrogenase from rat liver has been determined, showing the mature polypeptide to consist of 513 amino acid residues, with an acyl‐blocked N‐terminus. This structure is homologous to those of both other eutherian and marsupial mammals (human and opossum), thus characterizing a mammalian type enzyme to which the human form, notwithstanding its large number of genetic variants, conforms. The mammalian type differs from the fruit fly enzyme by about 50%. Known mutant forms exhibit further differences, widely distributed along the polypeptide chain. Structural patterns show glucose‐6‐phosphate dehydrogenases to consist of a few variable regions intermixed with relatively constant segments.