Arthrobacter oxydans as biocatalyst for purine deamination

ROSARIO MEDICI; ELIZABETH S. LEWKOWICZ; ADOLFO M. IRIBARREN

FEMS MICROBIOLOGY LETTERS

WILEY-BLACKWELL PUBLISHING, INC

Año: 2008 vol. 289 p. 20 - 26

0378-1097

Deaminases are enzymes that catalyze the hydrolysis of amino groups of nucleosidesor their bases. Because these enzymes play important roles in nucleotidemetabolism, they are relevant targets in anticancer and antibacterial therapies.Mammalian deaminases are commercially available but the use of bacterial wholecells, especially as biocatalysts, is continuously growing because of their economicalbenefits. Moreover, deaminases are useful for the preparative chemoenzymatictransformation of nucleoside and base analogues into a variety of derivatives. Thepurine deaminase activities of Arthrobacter oxydans, a gram-positive bacteriumutilized widely in bioremediation, were studied. The presence of adenosine,adenine and guanine deaminases was demonstrated and some purine bases andnucleosides were analyzed as substrates. Using A. oxydans whole cells as thebiocatalyst, different purine compounds such as the anti-HIV, 20,30-dideoxyinosine(73%, 2 h) were obtained.