The Site of Cleavage on Escherichia coli Glutamine Synthetase by Dithiotreitol, Fe (III) and O_2

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.
Publisher
Wiley-Blackwell
Issue Date
1991
Language
ENG
Keywords

MIXED-FUNCTION OXIDATION; PROTEINS; INACTIVATION; ENZYMES; SEQUENCE

Citation

BIOFACTORS, v.3, no.2, pp.121 - 125

ISSN
0951-6433
URI
http://hdl.handle.net/10203/57314
Appears in Collection
BS-Journal Papers(저널논문)
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