title: [The nature of functional groups in the active center of antitumor glutamin-(asparagin-)ase].
abstract: The effect of two reagents on glutamin (asparagin) ase from Pseudomonas aurantiaca-548 has been studied. 2,3-butanedione which modified arginine residues was ineffective for the inactivation of the enzyme. The enzyme was completely inactivated in the presence of N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K). The effects of pH, reagent concentration, competitive inhibitors and their analogues on the rate or degree of enzyme inactivation were studied. The experimental results suggest that the carboxyl groups localized at the active site of glutamin (asparagin) ase are probably essential for the substrate binding.
authors: Z I
authors: ZI
authors: Lebedeva
authors: E A
authors: EA
authors: Kabanova
authors: T T
authors: TT
authors: Berezov
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D000970:Antineoplastic Agents; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004852:Epoxy Compounds; D007202:Indicators and Reagents; D007555:Isoxazoles; D011549:Pseudomonas / Q000201:enzymology
chemical_list: D000970:Antineoplastic Agents; D004791:Enzyme Inhibitors; D004852:Epoxy Compounds; D007202:Indicators and Reagents; D007555:Isoxazoles; C009686:N-ethyl-5-phenylisoxazolium-3'-sulfonate; C007366:diepoxybutane; D000581:Amidohydrolases; C020654:glutamin-(asparagin-)ase
vernacular_title: O prirode funktsional'nykh gruppy aktivnogo tsentra antiopukholevoĭ glutamin(asparagin)azy.