The sites of cleavage on Escherichia coli glutamine synthetase by dithiothreitol, Fe(III) and O2.
Native conformation of an enzyme molecule is required for the specific non-enzymatic cleavage of Escherichia coli glutamine synthetase by a metal-catalyzing oxidation system comprised of dithiothreitol, Fe(III) and O2. The cleavage reaction is greatly inhibited by the addition of Mg(II). Two major cleavage sites are identified between amino acid residues 264 and 268, and roughly between amino acid residues 31 and 34, which are located on the protein segments forming the active site of the enzyme. These results suggest that the cleavage reaction is a largely site-specific process involving active oxygen species generated at the divalent cation binding sites on glutamine synthetase.
Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Seoul.
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Jhon
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Kim
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Byun
D001665:Binding Sites; D004229:Dithiothreitol / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D005290:Ferric Compounds / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D011487:Protein Conformation
D005290:Ferric Compounds; D005974:Glutamate-Ammonia Ligase; D010100:Oxygen; D004229:Dithiothreitol