[Some properties of beta-aspartate kinase from Micrococcus glutamicus-95 bacteria].
Kinetic and allosteric properties of beta-asparatatekinase from Micrococcus glutamicus-95 were studied. Coarse protein fraction, sedimented at 0.8 from saturated (NH4)2SO4, was used as an enzyme preparation. Curves of the dependency of the enzymatic reaction rate on substrate (L-aspartic acid and ATP) concentration were not found to be S-like. However, double reciprocal plotting of the data obtained revealed their deviation from the hyperbolic curve. The effect of amino acids (lysine, threonine, isoleucine, valine) on the activity of beta-aspartatekinase is studied. Lysine was shown to inhibit slightly beta-aspartatekinase, while threonine slightly activated it. Combined addition of both amino acids at a concentration of 1 mM resulted in the 50% inhibition. Isoleucine and valine activated beta-aspartatekinase and eliminated multivalent inhibitory effect of lysine and threonine. Interaction of isoleucine and lysine+threonine with beta-aspartatekinase was competitive with respect to L-aspartic acid and non-competitive in relation to ATP.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000596:Amino Acids / Q000494:pharmacology; D001222:Aspartate Kinase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000494:pharmacology*; D001224:Aspartic Acid / Q000494:pharmacology; D003470:Culture Media; D004789:Enzyme Activation / Q000187:drug effects; D004794:Enzyme Repression / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008837:Micrococcus / Q000201:enzymology*; D009154:Mutation; D010770:Phosphotransferases / Q000494:pharmacology*; D013053:Spectrophotometry
D000596:Amino Acids; D003470:Culture Media; D001224:Aspartic Acid; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D001222:Aspartate Kinase
Nekotorye svoĭstva beta-aspartatkinazy bakteriĭ Micrococcus glutamicus-95