Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties.
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.
Orth
T
T
Chemistry Department, M.V. Lomonosov Moscow State University, Russia.
Voronov
S
S
Binevski
P
P
Saenger
W
W
Kost
O
O
D000818:Animals; D002384:Catalysis; D002417:Cattle; D004795:Enzyme Stability; D006031:Glycosylation; D008168:Lung / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013379:Substrate Specificity
D007703:Peptidyl-Dipeptidase A