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Literature summary for 6.3.1.2 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
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Protein Variants

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

pH Optimum

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