[Irreversible inactivation of Chlorella glutamine synthetase by urea].
The effect of urea on Chlorella glutamine synthetase (E. C. 6.3.1.2) activity and tertiary structure is investigated. Urea is found to inhibit the activity of glutamine synthetase, the inhibitory effect being independent on the time. The enzyme molecule relax and changes its affinity to ammonium under the effect of urea at concentrations of 1.0-4.0 M. Higher concentrations of urea (5,0 M and more) produce a dissociation of the enzyme molecule into monomers without any intermediate forms. Monomers do not possess any synthetase and transferase activities. Substrates and cofactors do not protect the enzyme from the effect of urea and do not stimulate the emzyme reactivation and reaggregation after its dissotiation. The data obtained are discussed from the viewpoint of the regulation of Chlorella glutamine synthetase activity in vivo.
D000818:Animals; D002708:Chlorella / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors*; D007700:Kinetics; D046911:Macromolecular Substances; D014508:Urea / Q000494:pharmacology*
D046911:Macromolecular Substances; D014508:Urea; D005974:Glutamate-Ammonia Ligase
Neobratimaia inaktivatsiia glutaminsintetazy khlorelly mochevinoĭ.