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  • Title: Subunit interaction elicited by partial inactivation with L-methionine sulfoximine and ATP differently affects the biosynthetic and gamma-glutamyltransferase reactions catalyzed by yeast glutamine synthetase.
    Author: Kim KH, Rhee SG.
    Journal: J Biol Chem; 1987 Sep 25; 262(27):13050-4. PubMed ID: 2888756.
    Abstract:
    Yeast glutamine synthetase can be irreversibly inactivated in the presence of L-methionine sulfoximine, ATP, and a divalent cation Mn2+ or Mg2+. Kinetic studies with partially inactivated enzymes show that inactivation of a given subunit in the octameric glutamine synthetase affects the activities of its neighboring subunit such that the rate of the inactivation as well as the gamma-glutamyltransferase activity of the noninactivated subunits decreases while their biosynthetic activity is enhanced. This outcome of subunit interaction is the same irrespective of whether Mn2+ or Mg2+ is used to fulfill the divalent cation requirement of glutamine synthetase for the inactivation reaction and the gamma-glutamyltransferase reaction. Although only Vmax is affected in the gamma-glutamyltransferase assay, both Km (glutamate) and Vmax are changed in the biosynthetic assay.
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