dipeptidyl hydroxamic acids (H-X-Gly-NHOH: X = amino acid residues) was synthesized, and the inhibitory activity against Jackbean and Proteus mirabilis ureases [EC3.5.1.5] was examined. A number of H-X-Gly-NHOH inhibited Jackbeanurease 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 Jackbeanurease was more potent
[reaction: see text] A one-step conversion of carboxylic acids to hydroxamicacids under very mild conditions is described. This simple and efficient method has been applied for the synthesis of enantiopure hydroxamate of alpha-amino acids and peptides.