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Eur J Biochem. 1989 Dec 22;186(3):551-6.

Glucose-6-phosphate dehydrogenase. Characteristics revealed by the rat liver enzyme structure.

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1
Department of Biochemistry, University of Aberdeen, Marischal College, Scotland.

Abstract

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.

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