title: Carbohydrates regulate the dimerization of angiotensin-converting enzyme.
abstract: Regulation of the catalytic activity and supramolecular structure of angiotensin-converting enzyme was studied in reverse micelles of Aerosol OT in octane as biomembrane model. The kinetic experiments and the sedimentation analysis demonstrated that the enzyme can function both in monomeric and dimeric form. The degree of dimerization was strongly dependent on the concentration and structure of mono- and disaccharides added to the media, indicating the specific role of carbohydrates in forming the supramolecular structure of angiotensin-converting enzyme. The existence of carbohydrate-binding center on the enzyme molecule is proposed.
authors.affiliation: Department of Chemistry, Moscow State University, Russian Federation. kost@enzyme.chem.msu.su
authors.forename: O A
authors.initials: OA
authors.lastname: Kost
authors.forename: T A
authors.initials: TA
authors.lastname: Orth
authors.forename: I I
authors.initials: II
authors.lastname: Nikolskaya
authors.forename: S N
authors.initials: SN
authors.lastname: Nametkin
authors.forename: A V
authors.initials: AV
authors.lastname: Levashov
mesh_terms: D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry / Q000494:pharmacology*; D002417:Cattle; D019281:Dimerization; D008168:Lung / Q000737:chemistry; D008823:Micelles; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D002241:Carbohydrates; D008823:Micelles; D007703:Peptidyl-Dipeptidase A