Crystalline quinolinate phosphoribosyltransferase. II. Properties of the enzyme.
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Biomedical subjects
Publications and source records attributed to W B Jakoby.
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Crystals of thyroglobulin have been obtained from ammonium sulfate solutions and have been examined by electron microscopy as shadowed carbon replicas. Unit size in the crystal is 228 +/- 9 angstroms, which corresponds to a molecular weight of 5,300,000. Data are in accord with the possibility that this unit represents a polymer of thyroglobulin.
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The sulfotransferases that are active in the metabolism of xenobiotics represent a large family of enzymes that catalyze the transfer of the sulfuryl group from 3'-phosphoadenosine 5'-phosphosulfate to phenols, to primary and secondary alcohols, to several additional oxygen-containing functional groups, and to amines. Restriction of this review to the catalytic processes of phenol or aryl sulfotransferases does not really narrow the field, because these enzymes have overlapping specificity, not only for specific compounds, but also for multiple functional groups. The presentation aims to provide an overview of the wealth of phenol sulfotransferases that are available for study but concentrates on the enzymology of rat and human enzymes, particularly on the predominant phenol sulfotransferase from rat liver. The kinetics and catalytic mechanism of the rat enzyme is extensively reviewed and is compared with observations from other sulfotransferases.