Deoxyhypusine hydroxylase from rat testis. Partial purification and characterization.
作者： Myung Hee Park , J. E. Folk , A. Abbruzzese
DOI: 10.1016/S0021-9258(17)35750-2
关键词: Deoxyhypusine synthase 、 Hydroxylation 、 EIF5A 、 Deoxyhypusine Hydroxylase 、 Biology 、 Ascorbic acid 、 Oxidoreductase 、 Biochemistry 、 Hypusine 、 Molecular biology 、 Enzyme
摘要: Deoxyhypusine hydroxylase, the enzyme that catalyzes formation of hypusine from deoxyhypusine in eukaryotic initiation factor 4D, has been partially purified rat testis. The requires only addition certain sulfhydryl compounds for catalytic activity, dithiothreitol being most effective. Its lack dependency on alpha-keto acid-dependent dioxygenase cofactors, Fe2+, alpha-ketoglutarate, and ascorbic acid, its failure to decarboxylate stoichiometrically alpha-ketoglutarate with hydroxylation, strong specific inhibition by Fe2+ all suggest a mechanism this unlike prolyl lysyl hydroxylases.
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