Structural organization of membrane and soluble forms of somatic angiotensin-converting enzyme.

The catalytic activity and quaternary structure of soluble (s) and membrane (m) forms of angiotensin-converting enzyme (ACE) were studied in reversed micelles of ternary system Aerosol OT--water--octane. The profile of the dependence of the catalytic activity of the two enzyme forms on the degree of surfactant hydration (micellar size) had several optima corresponding to the function of various active oligomeric enzyme forms; the curves for the s- and m-forms of ACE were different. Data of sedimentation analysis prove that in reversed micelles, s-ACE can exist as monomers, dimers, or tetramers depending on the hydration degree, and the m-form is present as dimers and tetramers only. The values of the kinetic parameters for the hydrolysis of the substrate furylacryloyl-Phe-Gly-Gly by all the enzyme forms were determined, and the data indicate that the activity of the m-form is enhanced by oligomerization. The ACE activity strongly depends on the medium; it is higher when ACE is in contact with matrix or other enzyme molecules.