New feature of angiotensin-converting enzyme: carbohydrate-recognizing domain
Related Experiment Video
Updated: Oct 10, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
O A Kost1, N V Bovin, E E Chemodanova
1Chemistry Department, MV Lomonosov Moscow State University, Russia. kost@enzyme.chem.msu.ru
Abstract:
Self carbohydrate-mediated dimerization of glycoprotein angiotensin-converting enzyme (ACE) was demonstrated. The dimerization was studied in the reverse micelle experimental system as a model of biomembrane situation. Asialo-ACE or agalacto-ACE was able to form a dimer, whereas deglycosylated ACE and sequentially desialylated and degalactosylated ACE failed to dimerize. ACE-ACE interaction was competitively inhibited by Neu5Ac- or Gal-terminated saccharides. The results have allowed us to propose the existence of carbohydrate-recognizing domain (CRD) on ACE molecule. The structural requirements of this CRD were estimated based on the ability of saccharides to inhibit ACE dimerization. The most effective monosaccharides with equal inhibition potencies were shown to be galactose (as GalbetaOMe) and N-acetylneuraminic acid (as Neu5AcalphaOMe). Among oligosaccharides, the most effective ones were found to be 3'SiaLac and, especially, the whole pool of ACE oligosaccharide chains and biantennae complex oligosaccharide chains of other glycoproteins. Bovine and human ACEs were shown to be similar in terms of recognition of carbohydrates.
Related Concept Videos
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors
Protein Glycosylation
Glycosylation occurs in...
Tail-anchoring of Proteins in the ER Membrane
Enzyme-linked Receptors
Antihypertensive Drugs: Angiotensin II Receptor Blockers

