Isolation and characterization of the orotidine 5'-monophosphate decarboxylase domain of the multifunctional protein uridine 5'-monophosphate synthase.
作者： E E Floyd , M E Jones
DOI: 10.1016/S0021-9258(17)39386-9
关键词:
摘要: Abstract The multifunctional protein uridine 5'-monophosphate (UMP) synthase catalyzes the final two reactions of de novo biosynthesis UMP in mammalian cells by sequential action orotate phosphoribosyltransferase (EC 2.4.2.10) and orotidine (OMP) decarboxylase 4.1.1.23). This is composed one or identical subunits; monomer weighs 51,500 daltons. from mouse Ehrlich ascites can exist as three distinct species determined sucrose density gradient centrifugation: a 3.6 S monomer, 5.1 dimer, 5.6 conformationally altered dimer. Limited digestion each these with trypsin produced 28,500-dalton peptide that was relatively resistant to further proteolysis. appears be enzyme domains for it retained only OMP activity. Similar results were obtained when digested elastase. activity less stable domain than synthase; rapidly lose upon storage dilution. size similar yeast decarboxylase. If polypeptides which are cleaved derived exclusively either amino carboxyl end synthase, then fragment possessing could large 23,000 daltons Escherichia coli.
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