[Inhibition of bacterial agmatinase by substrate analogs].

Activity of agmatinase (EC 3.5.3.11) from Proteus vulgaris was studied in presence of guanidine derivatives of agmatine as substrates. The guanidine derivatives, containing carboxyl group, did not interact with the enzyme. An inhibitory effect developed if the carboxyl group was esterified. For exhibition of the effect the length of hydrocarbon radical in ligand and presence of hydrophobic groups were important. One of the most effective inhibitor was N-isoamylene agmatine (K1=0.001 M). Compounds, containing an amino- or guanidine group at the position opposite to the guanidine end and possessing the hydrocarbon chain not less that C4 were shown to be substrates of agmatinase.