[Interaction between dialkylamines and bacterial agmatinase].

It was demonstrated that aliphatic dialkylamines are more effective inhibitors of bacterial agmatinase than monoalkylamines and differ from the latter by the type of inhibition. The dependence of the inhibition constant on the hydrophobicity of the compounds tested was studied. The type of this dependence was found to be different for long- and short-radical dialkylamines, the correlation equation appearing as 1g(1/Ki) = 0,33 1gPo + (2,3 +/- 0,2) for the former compounds and as 1g(1/Ki) = 1,0 1gPo + (2,2 +/- 0,2) for the latter. The enzyme inhibition by the inhibitors tested was dependent on pH: e. g. with an increase in pH the inhibiting effect was decreased. It was assumed that the inhibitor sorption by agmatinase is of hydrophobic-ionic type and that the active site of the enzyme contains two hydrophobic zones separated by a nucleophylic group. The length of the hydrophoblic zones was estimated.