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Carbohydrates regulate the dimerization of angiotensin‐converting enzyme
Author(s) -
Kost Olga A.,
Orth Tatyana A.,
Nikolskaya Irina I.,
Nametkin Sergei N.,
Levashov Andrey V.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201572
Subject(s) - enzyme , monomer , chemistry , micelle , supramolecular chemistry , structure function , catalysis , biochemistry , angiotensin converting enzyme , biophysics , stereochemistry , molecule , organic chemistry , biology , polymer , physics , particle physics , aqueous solution , blood pressure , endocrinology
Abstract Summary. 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.