1. [Untitled]
- Author
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Bang-Ho Song, Ju-Hyung Woo, Sa-Youl Ghim, Tae-Ho Kim, Jong-Guk Kim, Hyun-Jeung Shin, and Lak-Shin Jeong
- Subjects
chemistry.chemical_classification ,Lysis ,Bacillaceae ,biology ,Deamination ,Lamivudine ,Bioengineering ,General Medicine ,Cytidine deaminase ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Bacillales ,law.invention ,Enzyme ,Biochemistry ,chemistry ,law ,Recombinant DNA ,medicine ,Biotechnology ,medicine.drug - Abstract
To decrease the costs of producing the anti-HIV drug, lamivudine, an enzymatic conversion process was developed instead of the traditional chemical method. Thermostable cytidine deaminase was over-produced by cloning the cdd gene into E. coli JF611/pCJH53 from Bacillus caldolyticus. The purified cytidine deaminase was recovered from the lysate of the recombinant E. coli JF611/pCJH53 by removing heat-denatured proteins and eluting sequential chromatography. When the enzyme was used to deaminate (−)-β-l-(2R, 5S)- and (+)-β-d-(2S, 5R)-1, 3-oxathiolanyl-cytosine, about 68% of the (+)-β-d-(2S, 5R)-1, 3-oxathiolanyl-cytosine was deaminated into the corresponding (+)-thiauridine maximally.
- Published
- 2001
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