The biosynthesis of protein-bound hypusine (N epsilon -(4-amino-2-hydroxybutyl)lysine). Lysine as the amino acid precursor and the intermediate role of deoxyhypusine (N epsilon -(4-aminobutyl)lysine).

摘要: The major labeled constituent produced in cellular protein during the incubation of Chinese hamster ovary (CHO) cells with [3H]putrescine or [terminal methylenes-3H]spermidine was identified as hypusine (N epsilon -(4-amino-2-hydroxybutyl)lysine). This unusual amino acid found to occur predominantly one relatively acidic low molecular weight protein. When CHO were [4,5-3H)lysine, a small portion radioactivity fraction, after release by proteolytic digestion hydrolysis, chromatographed at position hypusine. Oxidative degradation this isolated material yielded lysine, thus, providing evidence that lysine is precursor Upon metal chelator, alpha,alpha-dipyridyl, and either [4,5]3H]lysine methylenes-3H]spermidine, label incorporated into protein-bound material, chromatographic properties which, digestion, be different from those cell unhydroxylated form hypusine, deoxyhypusine -(4-aminobutyl)lysine). Evidence normal biosynthesis proceeds through hydroxylation obtained demonstration conversion both intact cell-free lysate. In presence accumulated single whose two dimensional electrophoretic indistinguishable usual hypusine-containing finding supports proposed mechanism which peptide-bound converted transitory intermediate, deoxyhypusine.