[Inactivation of microbial glutamin-(asparagin-)ase by azaserine and 6-diazo-5-oxo-L-norleucine].
The effect of substrate analogues on glutamin-(asparagin-)ase from Pseudomonas aurantiaca-548 has been studied. The enzyme was demonstrated to be highly sensitive to the the action of 6-diazo-5-oxo-L-norleucine and azaserine. L-isomers of glutamine, aspartate, glutamate and several other substrate analogues with free alpha-amino groups protected the enzyme against the inhibitory DON effect. Thus, thorough preliminary selection of appropriate inhibitors, their dosage and treatment duration is needed for the recommendation of combined enzyme-inhibitor application in anti-tumour chemotherapy.
D000581:Amidohydrolases / Q000037:antagonists & inhibitors*; D000970:Antineoplastic Agents; D001377:Azaserine / Q000494:pharmacology*; D001391:Azo Compounds / Q000494:pharmacology*; D003980:Diazooxonorleucine / Q000494:pharmacology*; D011549:Pseudomonas / Q000187:drug effects / Q000201:enzymology; D013379:Substrate Specificity / Q000187:drug effects
D000970:Antineoplastic Agents; D001391:Azo Compounds; D003980:Diazooxonorleucine; D001377:Azaserine; D000581:Amidohydrolases; C020654:glutamin-(asparagin-)ase
Inaktivatsiia mikrobnoĭ glutamin(asparagin)azy azaserinom i 6-diazo-5-okso-L-norleĭtsinom.