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REVIEW: L-Lysine alpha-Oxidase: Physicochemical and Biological Properties

E. V. Lukasheva* and T. T. Berezov

Department of Biochemistry, Russian Peoples' Friendship University, ul. Miklukho-Maklaya 8, Moscow, 117198 Russia; fax: (095) 434-0412; E-mail: lukashev@aha.ru

* To whom correspondence should be addressed.

Received April 17, 2002; Revision received June 10, 2002
This review summarizes data on the properties of L-lysine alpha-oxidase, an enzyme that belongs to the group of oxidases of L-amino acids. This enzyme acts virtually only on L-lysine with a rather low Km yielding alpha-keto-epsilon-aminocaproic acid. The decrease in the level of the essential amino acid L-lysine and the formation of hydrogen peroxide during the reaction possibly provide the basis for the unique properties of L-lysine alpha-oxidase: cytotoxic, antitumor, antimetastatic, antiinvasive, antibacterial, and antiviral activities, as well as an immunomodulating effect. Native L-lysine alpha-oxidase and its immobilized forms are promising tools for determination of concentration of L-lysine in various biological materials.
KEY WORDS: L-lysine alpha-oxidase, L-amino acid oxidase, immobilized enzymes, L-lysine assay, enzymes in medicine, antitumor enzyme, antiviral enzyme, antibacterial enzyme, antiinvasive effect, antimetastatic effect, soluble enzyme conjugates, enzyme conjugated with monoclonal antibodies to tumor cell receptors