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.
Chemistry Department, M.V. Lomonosov Moscow State University, Russia.
T
T
Orth
S
S
Voronov
P
P
Binevski
W
W
Saenger
O
O
Kost
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