Title : Structure activity relationship of phosphoramidon derivatives for in vivo endothelin-converting-enzyme inhibition.

Pub. Date : 1994

PMID : 8020872






4 Functional Relationships(s)
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1 The structure activity relationship of phosphoramidon analogues was studied for their ability to reduce the hypertensive effect of exogenous proET-1, probably via inhibition of an endothelin converting enzyme activity (ECE). phosphoramidon endothelin converting enzyme 1 Homo sapiens
2 Furthermore, the tryptophan residue of phosphoramidon appeared to be particularly important for the ECE inhibition, whereas thermolysin inhibition seemed to depend greatly on the leucine residue. phosphoramidon endothelin converting enzyme 1 Homo sapiens
3 It is concluded that in vivo ECE and thermolysin differ in the way they recognise phosphoramidon. phosphoramidon endothelin converting enzyme 1 Homo sapiens
4 The existence of an hydrophobic pocket, specific for the recognition of the tryptophan residue of phosphoramidon, could be proposed for ECE. phosphoramidon endothelin converting enzyme 1 Homo sapiens