Abstract
Glutamine synthetase [EC 6.3.1.2] from yeast (Saccharomyces cerevisiae) was purified to a homogeneous state both ultracentrifugally and electrophoretically. The enzyme has a molecular weight of 630,000 and a sedimentation coefficient (S20,W0.2%) of 18.9S. The molecular weight of the subunit dissociated by 0.1% sodium dodecyl sulfate containing 1 mM 2-mercaptoethanol is 61,000, which suggests the presence of 10 sub-units in the native molecule. The amino acid composition is similar to those of the enzymes from E. coli, B. subtilis, and B. stearothermophilus. The enzyme requires divalent cations such as Mg2+ and Mn2+ for activity. The enzyme can use D-glutamic acid as a substrate in place of L-glutamic acid. Glycine, alanine, tryptophan, histidine, AMP, and CTP all inhibit the enzyme activity to various extents.
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