Renalase, a new secretory enzyme responsible for selective degradation of catecholamines: Achievements and unsolved problems

• Published in: Biochemistry (Moscow) Vol. 75; no. 8; pp. 951 - 958
• Main Authors: Medvedev, A. E, Veselovsky, A. V, Fedchenko, V. I
• Format: Journal Article
• Language: English
• Published: Dordrecht Dordrecht : SP MAIK Nauka/Interperiodica 01-08-2010; SP MAIK Nauka/Interperiodica; Springer; Springer Nature B.V
• Subjects: Amino acids; Analysis; Animals; Biochemistry; Biodegradation; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Blood; Catalytic Domain; Catecholamines; Catecholamines - metabolism; Enzymes; Flavin-Adenine Dinucleotide - metabolism; Genes; Humans; Hypertension; Life Sciences; Microbiology; Monoamine Oxidase - blood; Monoamine Oxidase - chemistry; Monoamine Oxidase - urine; Protein Conformation; Review; Structure-Activity Relationship; catecholamines; enzymatic degradation; renalase; bioinformation analysis of amino acid sequence; structure; function
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297910080018

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.