Voprosy meditsinskoi khimii (ISSN 0042-8809)

Inhibition of bacterial agmatinase by substrate analogs

   
Khramov V.A.
PubMed Id: 17224
Year: 1976 vol: 22  issue:6  pages: 804-808
Abstract: 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.
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Reference: Khramov V.A., Inhibition of bacterial agmatinase by substrate analogs, Voprosy meditsinskoi khimii, 1976, vol: 22(6), 804-808.
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