Glucose-6-phosphate dehydrogenase. Characteristics revealed by the rat liver enzyme structure.
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.
Jeffery
J
J
Department of Biochemistry, University of Aberdeen, Marischal College, Scotland.
Barros-Söderling
J
J
Murray
L
L
Wood
I
I
Hansen
R
R
Szepesi
B
B
Jörnvall
H
H
D000595:Amino Acid Sequence; D000818:Animals; D005954:Glucosephosphate Dehydrogenase / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D005954:Glucosephosphate Dehydrogenase