Title : Inhibition and active-site modelling of prolidase.

Pub. Date : 1989 Mar 15

PMID : 2924773






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme. azetidine peptidase D Homo sapiens
2 Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme. pyrrolidine peptidase D Homo sapiens
3 Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme. piperidine peptidase D Homo sapiens
4 One of these, N-benzyloxycarbonyl-L-proline, was shown to be a potent competitive inhibitor of porcine kidney prolidase (Ki = 90 microM); its rapid protein-mediated permeation of human and sheep erythrocytes suggests that it may be effective in vivo. carbobenzoxyproline peptidase D Homo sapiens
5 Analysis of inhibitor action and consideration of X-ray crystallographic data of relevant Mn2+ complexes allowed the active-site model of prolidase to be further refined; a new model is presented in which the substrate acts as a bidentate ligand towards the active-site manganous ion. Manganese(2+) peptidase D Homo sapiens