Glucose‐6‐phosphate dehydrogenase
Open Access
- 1 December 1989
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 186 (3) , 551-554
- https://doi.org/10.1111/j.1432-1033.1989.tb15242.x
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.This publication has 33 references indexed in Scilit:
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