Specific Inhibition of Urease by N-Acylphosphoric Triamides (original) (raw)

Journal Article

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Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University

Sugitani, Toyama, Toyama 930-01

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Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University

Sugitani, Toyama, Toyama 930-01

Search for other works by this author on:

Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University

Sugitani, Toyama, Toyama 930-01

Search for other works by this author on:

Published:

01 December 1985

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Abstract

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2–21 nM, which are about 1,000-fold lower than that of caprylohydroxan-amic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, α-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, γ-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 μM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 μM and 54 μM, respectively, when acetyicholine was used as a substrate. These results show that _N_-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.

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© 1985, by the Japanese Biochemical Society

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