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Literature summary extracted from

  • Luo, S.; Kim, G.; Levine, R.L.
    Mutation of the adenylylated tyrosine of glutamine synthetase alters its catalytic properties (2005), Biochemistry, 44, 9441-9446.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.2 Y397A mutant enzyme behaves as if it is adenylated Escherichia coli
6.3.1.2 Y397F the specific activity is almost double that of the wild-type enzyme, mutant enzyme behaves as if it is unadenylated Escherichia coli
6.3.1.2 Y397S mutant enzyme behaves as if it is adenylated Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.1.2 AMP no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form Escherichia coli
6.3.1.2 CTP no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form Escherichia coli
6.3.1.2 His no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form Escherichia coli
6.3.1.2 Trp no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.2 Mg2+ gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated Escherichia coli
6.3.1.2 Mn2+ gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.2 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.2
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.1.2 6.9
-
 adenylated enzyme, Mn2+-dependent activity Escherichia coli
6.3.1.2 8
-
 unadenylated enzyme, Mn2+-dependent activity Escherichia coli