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. 1974 May;71(5):1767–1770. doi: 10.1073/pnas.71.5.1767

The Quaternary Structure of δ-Aminolevulinic Acid Dehydratase from Bovine Liver

Wen H Wu *,§, David Shemin *,§, Kenneth E Richards †,‡, Robley C Williams †
PMCID: PMC388320  PMID: 4525290

Abstract

The quaternary structure of δ-aminolevulinic acid dehydratase (5-aminolaevulinate hydrolyase, EC 4.2.1.24) from bovine liver was examined by analytical ultracentrifugation, polyacrylamide gel electrophoresis, and electron microscopy. The molecular weights, determined by sedimentation-velocity and sedimentation-equilibrium experiments, were 289,000 and 282,000, respectively. The molecular weight of the subunit in 6 M guanidine. HCl was 34,900 as determined by sedimentation-equilibrium and 35,000 as estimated by polyacrylamide gel electrophoresis. No evidence was obtained for the presence of a smaller polypeptide. It appears therefore that δ-aminolevulinic acid dehydratase from liver is composed of eight subunits. The molecules of the enzyme deposited in thin layers of negative stain were generally square with an edge length of 85-90 Å. On the assumption that the subunits are spherical in shape with a diameter of 44 Å and a density of 1.36 g/cm3, the molecular weight of the octamer is calculated to be 292,000. The particles appear to consist of four discrete lobes arrayed at the four corners of a square. The above conclusion that the dehydratase possesses eight subunits can be readily reconciled with the appearance of the enzyme in the electron microscope if it is postulated that the eight subunits are arranged at the corners of a cube. Therefore, it would follow that the subunits are arranged with dihedral (D4) symmetry.

Keywords: subunits, porphobilinogen, δ-aminolevulinic acid, porphyrins, electron microscopy

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Selected References

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