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Published on: October 4, 2017
Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties
T Orth1, S Voronov, P Binevski
1Chemistry Department, M.V. Lomonosov Moscow State University, Russia.
Abstract:
To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different changes of catalytic properties in the reaction of the hydrolysis of N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme.
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