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Regulation of Catalytic Activity of Acid Phosphatase by Lipids in a Reverse Micellar System

E. V. Kudryashova*, V. L. Bronza, and A. V. Levashov

Department of Chemical Enzymology, Chemical Faculty, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: (495) 939-2742; E-mail: Helena_koudriachova@hotmail.com; vbronza@bruker.ru; levashov@hotbox.ru

* To whom correspondence should be addressed.

Received January 21, 2008; Revision received February 18, 2008
The influence of biomembrane lipids on the catalytic activity of a peripheral membrane enzyme, acid phosphatase (AP), was studied in a reverse micellar system. It was found that the interaction of AP with lipids led to a number of kinetic effects depending on lipid nature on enzyme function. The observed effects might be caused by the formation of lipoprotein complexes as well as by the influence of lipids on structure and properties of the micellar matrix. The results are important for clear understanding of molecular mechanisms of regulation of the catalytic activity of the membrane-associated enzyme in vivo. These data can also be used as a physicochemical basis for application of AP in medical fields as a diagnostic tool for diseases caused by changes in lipid metabolism, e.g. urinary, orthopedic, and allergic diseases.
KEY WORDS: acid phosphatase, reverse micelles, lipids, catalytic activity, secondary structure

DOI: 10.1134/S0006297909030146