| Literature DB >> 15381315 |
M Andújar-Sánchez1, A Cámara-Artigas, V Jara-Pérez.
Abstract
The angiotensin I-converting enzyme (ACE; EC.3.4.15.1) is a dipeptidyl carboxypeptidase that plays a central role in blood pressure regulation. The somatic form of the enzyme is composed of two highly similar domains, usually referred to as N and C domains, each containing one active site. Nevertheless, a 1:1 stoichiometry for the binding of lisinopril, captopril or enalaprilat to somatic pig lung ACE is shown by isothermal titration calorimetry (ITC) and enzymatic assays. The binding of the three inhibitors at neutral pH is very tight and the enthalpy changes are positive, indicating that the binding is entropically driven. The origin of this thermodynamic signature is discussed under the new structural information available.Entities:
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Year: 2004 PMID： 15381315 DOI： 10.1016/j.bpc.2004.05.011
Source DB: PubMed Journal: Biophys Chem ISSN： 0301-4622 Impact factor: 2.352