REVIEW: Renalase, a New Secretory Enzyme Responsible for Selective Degradation of Catecholamines: Achievements and Unsolved Problems

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A. E. Medvedev^*, A. V. Veselovsky, and V. I. Fedchenko

Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya ul. 10, 119121 Moscow, Russia; E-mail: professor57@yandex.ru

^* To whom correspondence should be addressed.

Received March 22, 2010; Revision received March 29, 2010

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Renalase is a recently discovered secretory enzyme responsible for selective degradation of blood catecholamines. The review summarizes literature data on expression of this enzyme and on its structure and functions. Special attention is paid to unsolved and questionable problems including: 1) prediction of the presence of FAD in the protein structure based on amino acid sequence similarity of renalase with known FAD-dependent enzymes; 2) identity of plasma and urinary renalase; 3) mechanism underlying conversion of inactive renalase into the active form.

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KEY WORDS: catecholamines, enzymatic degradation, renalase, structure, function, bioinformation analysis of amino acid sequence

DOI: 10.1134/S0006297910080018

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