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(-6) M and inhibited Proteus mirabilis urease with an I50 of the order of 10(-5) M. The inhibition against Jack bean urease was more potent than that with the corresponding aminoacyl hydroxamic acids (H-X-NHOH).
Odake
S
S
Research Institute, Fuji Chemical Industries, Ltd., Toyama, Japan.
Nakahashi
K
K
Morikawa
T
T
Takebe
S
S
Kobashi
K
K
D004151:Dipeptides / Q000737:chemistry / Q000494:pharmacology*; D007887:Fabaceae / Q000201:enzymology; D006801:Humans; D006877:Hydroxamic Acids / Q000737:chemistry / Q000494:pharmacology*; D010946:Plants, Medicinal; D011513:Proteus mirabilis / Q000201:enzymology; D014510:Urease / Q000037:antagonists & inhibitors* / Q000652:urine
D004151:Dipeptides; D006877:Hydroxamic Acids; D014510:Urease