Purification and properties of glutamine synthetase from Saccharomyces cerevisiae

J Biol Chem. 1983 Jan 10;258(1):119-24.


We have purified glutamine synthetase over 130-fold from Saccharomyces cerevisiae. The enzyme exhibits a Km for glutamate of 6.3 mM and a Km for ATP of 1.3 mM in the biosynthetic reaction, with a pH optimum from 6.1 to 7.0. Ten to twelve 43,000 molecular weight subunits comprise the active enzyme of 470,000 molecular weight. Rabbit antibodies prepared against the purified enzyme were used to show that induction of enzyme activity correlates with de novo synthesis of the enzyme subunit.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Glutamate-Ammonia Ligase / isolation & purification*
  • Glutamate-Ammonia Ligase / metabolism
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Saccharomyces cerevisiae / enzymology*


  • Macromolecular Substances
  • Glutamate-Ammonia Ligase