Some properties of Escherichia coli glutamine synthetase after limited proteolysis by subtilisin.

Anthranilate Synthetase From Escherichia coli SJHI: Purification and Some Properties

Abstract: A procedure employed in the purification of anthranilate synhetase of Escherichia coli SJHI is described. The purified anthranilate synthetase appeared to be homogeneous when examined with poliacrylamide gel electrophoresis. Phenly-sepharose CL-4B and Blue dye sepharose were used for purification. A positive correlation was found between purification and ammonium sulfate especially us...

Mn2+ and substrate interactions with glutamine synthetase from Escherichia coli.

Glutamine synthetase of pseudomonads: some biochemical and physicochemical properties.

The glutamine synthetases from several Pseudomonas species were purified to homogeneity, and their properties were compared with those reported for the enzymes from Escherichia coli and other gram-negative bacteria. The glutamine synthetase from Pseudomonas fluorescens was unique because it was nearly precipitated quantitatively as a homogeneous protein during dialysis of partially purified pre...

Regulation of glutamine synthetase. X. Effect of growth conditions on the susceptibility of Escherichia coli glutamine synthetase to feedback inhibition.

The kinetic properties of Escherichia coli glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors known to influence this enzyme; however, the enzyme from log-phase cells grown on glucose and growth-limiting concentrations...

Studies on glutamine synthetase from Escherichia coli. Formation of pyrrolidone carboxylate and inhibition by methionine sulfoximine.

Both the adenylylated and unadenylylated forms of Escherichia coli glutamine synthetase catalyze the formation of pyrrolidone carboxylate from glutamate in the presence of ATP and divalent metal ions (Mg++ or Mn++) and in the absence of ammonia. The unadenylylated enzyme catalyzes this reaction more rapidly with Mg++ than with Mn++, while the adenylylated enzyme catalyzes it more rapidly with M...