Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system.
The first step in the proteolytic degradation of bacterial glutamine synthetase is a mixed function oxidation of one of the 16 histidine residues in the glutamine synthetase subunit (Levine, R.L. (1983) J. Biol. Chem. 258, 11823-11827). A model system, consisting of oxygen, a metal ion, and ascorbic acid, mimics the bacterial system in mediating the oxidative modification of glutamine synthetase. This model system was studied to gain an understanding of the mechanism of oxidation and of factors which control the susceptibility of the enzyme to oxidation. Availability of substrates and the extent of covalent modification of the enzyme (adenylylation) interact to modulate susceptibility of the enzyme to oxidation. This interaction provides the biochemical basis for physiologic regulation of intracellular proteolysis of glutamine synthetase. The oxidative modification requires hydrogen peroxide. While the reaction may involve Fenton chemistry, the participation of free radicals, superoxide anion, and singlet oxygen could not be demonstrated.
D000596:Amino Acids / Q000494:pharmacology; D001205:Ascorbic Acid / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology; D005296:Ferrous Compounds / Q000494:pharmacology; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D006639:Histidine / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D000596:Amino Acids; D005296:Ferrous Compounds; D013438:Sulfhydryl Compounds; C020748:ferrous sulfate; D006639:Histidine; D006861:Hydrogen Peroxide; D005974:Glutamate-Ammonia Ligase; D001205:Ascorbic Acid