Inhibition of Urease Activity by Dipeptidyl Hydroxamic Acids.

Authors:
  • KNKazuaki Nakahashi
    Kazuaki Nakahashi
  • TMTadanori Morikawa
    Tadanori Morikawa
  • STSachiko Takebe
    Sachiko Takebe
  • KKKyoichi Kobashi
    Kyoichi Kobashi
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Abstract
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).