Inhibition of aminopeptidases by phosphonic acid and phosphinic acid analogues of aspartic and glutamic acids.
More than 30 phosphonic and phosphinic acid analogues of aspartic and glutamic acids were synthesized in order to probe how the structural differences of these molecules were reflected in their ability to inhibit cytosolic (LAP) and microsomal (APM) aminopeptidases. Although most of the compounds studied were found to exert only a modest inhibitory effect, the studies provide some information on the structural requirements of the binding subsites and catalytic centers of both enzymes.
Lejczak
B
B
Institute of Organic and Physical Chemistry, Technical University of Wroclaw, Poland.
De Choszczak
M P
MP
Kafarski
P
P
D000626:Aminopeptidases / Q000037:antagonists & inhibitors*; D000818:Animals; D001224:Aspartic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology; D005971:Glutamates / Q000737:chemistry / Q000494:pharmacology*; D018698:Glutamic Acid; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D063065:Organophosphonates / Q000737:chemistry / Q000494:pharmacology*; D010721:Phosphinic Acids / Q000737:chemistry / Q000494:pharmacology*; D013552:Swine
D005971:Glutamates; D063065:Organophosphonates; D010721:Phosphinic Acids; D001224:Aspartic Acid; D018698:Glutamic Acid; D000626:Aminopeptidases