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Published on: October 2, 2012
Arthrobacter oxydans as a biocatalyst for purine deamination
Rosario Médici1, Elizabeth S Lewkowicz, Adolfo M Iribarren
1Biotransformation Laboratory, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina.
Bacterial deaminases from Arthrobacter oxydans show potential as cost-effective biocatalysts for producing valuable compounds. These enzymes are crucial for nucleotide metabolism and have applications in anticancer and antibacterial therapies.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Deaminases are critical enzymes in nucleotide metabolism, making them significant targets for anticancer and antibacterial drug development.
- Bacterial whole cells are increasingly used as economical biocatalysts compared to mammalian enzymes.
- Deaminases facilitate chemoenzymatic synthesis of nucleoside and base analogue derivatives.
Purpose of the Study:
- To investigate the purine deaminase activities in the gram-positive bacterium Arthrobacter oxydans.
- To assess the potential of A. oxydans whole cells as biocatalysts for producing purine derivatives.
Main Methods:
- Enzyme assays were performed to detect adenosine, adenine, and guanine deaminase activities.
- Purine bases and nucleosides were used as substrates to analyze deaminase activity.
- Whole cells of A. oxydans were employed as biocatalysts for chemoenzymatic transformations.
Main Results:
- The presence of adenosine, adenine, and guanine deaminases was confirmed in A. oxydans.
- Various purine compounds were analyzed as substrates for the identified deaminases.
- The anti-HIV drug 2',3'-dideoxyinosine was synthesized with 73% yield in 2 hours using A. oxydans whole cells.
Conclusions:
- Arthrobacter oxydans possesses significant purine deaminase activities.
- Whole cells of A. oxydans are effective and economical biocatalysts for synthesizing purine derivatives.
- This study highlights the potential of bacterial deaminases in pharmaceutical synthesis and therapy development.
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