Lamivudine production via enantioselective deamination by thermostable Bacillus caldolyticus cytidine deaminase

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 cyt...

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Bibliographic Details
Published in:Biotechnology letters 2001-01, Vol.23 (2), p.131-135
Main Authors: WOO, Ju-Hyung, SHIN, Hyun-Jeung, KIM, Tae-Ho, GHIM, Sa-Youl, JEONG, Lak-Shin, KIM, Jong-Guk, SONG, Bang-Ho
Format: Article
Language:English
Subjects:
Antiviral drugs
Bacillus caldolyticus
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
cdd gene
Escherichia coli
Escherichia coli O157:H7
Fundamental and applied biological sciences. Psychology
Health. Pharmaceutical industry
Human immunodeficiency virus
Industrial applications and implications. Economical aspects
Lamivudine
Methods. Procedures. Technologies
Production of active biomolecules
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Summary: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 (-)- beta -L-(2R,5S)- and (+)- beta -D-(2S,5R)- 1,3-oxathiolanyl-cytosine, about 68% of the (+)- beta -D-(2S,5R)-1,3-oxathiolanyl-cytosine was deaminated into the corresponding (+)-thiauridine maximally.
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1010353502346