Analysis of latent properties of trypsin. Acyl trypsins derived from enantiomeric pairs of "inverse substrates".
p-Amidinophenyl esters derived from a variety of amino acids and peptides, including D-amino acids, were synthesized. The kinetic behavior of trypsin towards these esters, which are "inverse substrates," was analyzed. Deacylation rates of acyl trypsins carrying D-amino acid residues were determined for the first time by the use of these "inverse substrates." The steric requirements of the catalytic site region of trypsin were successfully analyzed by studying the deacylation process as manifested in the hydrolyses of enatiomeric pairs of "inverse substrates." The effects of chiral ligands on the deacylation process were also studied in connection with the chiral requirements of the active site.
D000215:Acylation; D000588:Amines / Q000494:pharmacology; D001665:Binding Sites; D007700:Kinetics; D013237:Stereoisomerism; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
D000588:Amines; D014357:Trypsin