70873-80-2Relevant articles and documents
Design of potent and specific inhibitors of carboxypeptidases A and B.
Ondetti et al.
, p. 1427,1428 (1979)
The combination in one molecule of functional groups that can interact specifically with different substrate binding areas at the active site of carboxypeptidases A and B has led to the development of potent and specific inhibitors of these enzymes. 2-Benzyl-3-mercaptopropanoic acid (SQ 14,603) has a Ki of 1.1 x 10(-8) M vs. carboxypeptidase A and a Ki of 1.6 x 10(-4) M vs. the B enzyme. 2-Mercaptomethyl-5-guanidinopentanoic acid (SQ 24,798) has a Ki of 4 x 10(-10) M vs. carboxypeptidase B and a Ki of 1.2 x 10(-5) M vs. carboxypeptidase A. It is proposed that the sulfhydryl groups of these inhibitors bind to the catalytically important zinc ions of these enzymes, and that, in conjunction with the benzyl and guanidinopropyl side chains, they are responsible for their specificity.
Amino acid derivatives
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, (2008/06/13)
A method for alleviating or reducing angiotensin related hypertension in hypertensive mammals comprises administering an effective amount of a compound having the general formula STR1 Intermediates for the preparation of such compounds are also included.
