| Autor: |
Ondetti MA, Condon ME, Reid J, Sabo EF, Cheung HS, Cushman DW |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 1979 Apr 17; Vol. 18 (8), pp. 1427-30. |
| DOI: |
10.1021/bi00575a006 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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