home   •   contacts
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Abstract
[print version] [full PDF]

O.A.Kost1*, N.V.Bovin2, E.E.Chemodanova1, V.V.Nasonov2, T.A.Orth1
New feature of  angiotensin-converting enzyme: carbohydrate-recognizing domain.
J. Mol. Recognit., 13 (6), pp. 360 - 369, (2000)

1 Chemistry Department, M.V.Lomonosov Moscow State University, Moscow, 119899, Russia
2 Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP-7, 117871

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 GalOMe) and N-acetylneuraminic acid (as Neu5AcOMe). Among oligosaccharides, the most effective ones were found to be 3SiaLac 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.

Keywords: angiotensin-converting enzyme, carbohydrates, lectins, reverse micelles


*To whom correspondence should be addressed: Chemistry Department, M.V.Lomonosov Moscow State University, Moscow, 119899, Russia, kost@enzyme.chem.msu.ru
research activity
publications
who is who
anti-spam policy
Laboratory of Carbohydrate Chemistry, IBChCopyright © 2005 - 2017. All rights reserved.