Inhibition of Urease Activity by Dipeptidyl Hydroxamic Acids

A series of dipeptidyl hydroxamic acids (H-X-Gly-NHOH : X=amino acid residues) was synthesized, and the inhibitory activity against Jack bean and Proteus mirabilis ureases [EC 3.5.1.5] was examined. A number of H-X-Gly-NHOH inhibited Jack bean urease with an I50 of the order of 10-6M and inhibited P...

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Veröffentlicht in:	Chemical & pharmaceutical bulletin 1992/10/25, Vol.40(10), pp.2764-2768
Hauptverfasser:	ODAKE, Shinjiro, NAKAHASHI, Kazuaki, MORIKAWA, Tadanori, TAKEBE, Sachiko, KOBASHI, Kyoichi
Format:	Artikel
Sprache:	eng
Schlagworte:	Chemistry dipeptide Dipeptides - chemistry Dipeptides - pharmacology Exact sciences and technology Fabaceae - enzymology Humans hydroxamic acid Hydroxamic Acids - chemistry Hydroxamic Acids - pharmacology inhibitor Organic chemistry Peptides Plants, Medicinal Preparations and properties Proteus mirabilis - enzymology urease Urease - antagonists & inhibitors Urease - urine
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Beschreibung
Zusammenfassung:	A series of dipeptidyl hydroxamic acids (H-X-Gly-NHOH : X=amino acid residues) was synthesized, and the inhibitory activity against Jack bean and Proteus mirabilis ureases [EC 3.5.1.5] was examined. A number of H-X-Gly-NHOH inhibited Jack bean urease with an I50 of the order of 10-6M and inhibited Proteus mirabilis urease with an I50 of the order of 10-5M. The inhibition against Jack bean urease was more potent than that with the corresponding aminoacyl hydroxamic acids (H-X-NHOH).
ISSN:	0009-2363 1347-5223
DOI:	10.1248/cpb.40.2764