caa a22 4500 467943435 CHVBK 20180405193734.0 cr unu---uuuuu 170328e20050101xx s 000 0 eng 10.1007/s10541-005-0050-2 doi (NATIONALLICENCE)springer-10.1007/s10541-005-0050-2 (NATIONALLICENCE)springer-10.1007/PL00021754 D-amino acid oxidase: structure, catalytic mechanism, and practical application [Elektronische Daten] [V. Tishkov, S. Khoronenkova] D-Amino acid oxidase (DAAO) is a FAD-dependent enzyme that plays an important role in microbial metabolism, utilization of endogenous D-amino acids, regulation of the nervous system, and aging in mammals. DAAO from yeasts Rhodotorula gracilis and Trigonopsis variabilis are used to convert cephalosporin C into 7-aminocephalosporanic acid, the precursor of other semi-synthetic cephalosporins. This review summarizes the recent data on the enzyme localization, physiological role, gene cloning and expression, and the studies on the enzyme structure, stability, catalytic mechanism, and practical applications. MAIK "Nauka/Interperiodica”, 2005 D-amino acid oxidase nationallicence cloning nationallicence expression nationallicence stability nationallicence protein engineering nationallicence Trigonopsis variabilis nationallicence Rhodotorula gracilis nationallicence DAAO : D-amino acid oxidase nationallicence DASPO : D-aspartate oxidase nationallicence pkDAAO : pig kidney D-amino acid oxidase nationallicence RgDAAO : D-amino acid oxidase from Rhodotorula gracilis nationallicence TvDAAO : D-amino acid oxidase from Trigonopsis variabilis nationallicence 7-ACA : 7-aminocephalosporanic acid nationallicence Tishkov V. Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia aut Khoronenkova S. Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia aut Biochemistry (Moscow) Nauka/Interperiodica 70/1(2005-01-01), 40-54 0006-2979 70:1<40 2005 70 10541 https://doi.org/10.1007/s10541-005-0050-2 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10541-005-0050-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tishkov V. Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia aut NATIONALLICENCE 700 1- Khoronenkova S. Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119992, Moscow, Russia aut NATIONALLICENCE 773 0- Biochemistry (Moscow) Nauka/Interperiodica 70/1(2005-01-01), 40-54 0006-2979 70:1<40 2005 70 10541 NATIONALLICENCE 856 40 https://doi.org/10.1007/PL00021754 text/html Onlinezugriff via DOI Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE NATIONALLICENCE NL-springer