Article
The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.
The Journal of biological chemistry - 5 Jul 1992
Wei L, Clauser E, Alhenc-Gelas F, Corvol P
Abstract excerpt
The endothelial angiotensin I-converting enzyme (ACE; EC 3.4.15.1) has recently been shown to contain two large homologous domains (called here the N and C domains), each being a zinc-dependent dipeptidyl carboxypeptidase. To further characterize the two active sites of ACE, we have investigated their interaction with four competitive ACE inhibitors, which are all potent antihypertensive drugs. The binding of...
Topics
- Angiotensin I
- Angiotensin-Converting Enzyme Inhibitors
- Animals
- Binding Sites
- CHO Cells
- Captopril
- Chlorides
- Cricetinae
- Enalapril
- Enalaprilat
- Humans