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KMID : 0364819880260040368
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Korean Journal of Microbiology
1988 Volume.26 No. 4 p.368 ~ p.374
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Enzymatic Properties of Extracelluiar Cytosine Deaminase
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Woo D. L.
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Abstract
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1
Enzymological proprties of an extracellular cytosine deaminase from Bacillus polymyxa YL 31-3 were investigated. The extraeellular enzyme was very stable, and optimum pH and temperature for the enzyme activity were found to be near pH 6.0 in 0.2M potassium phosphate buffer and at 30°C, respectively. 5-Fluorocytosine was converted to 5-fluoroursdi by the enzyme, but S-methykytosiae was not to thymine by it. The enzyme activity was completely inhibited by sons heavy metal ion such as 1mM of Cd2- and Hg2+, and by 1mM of p-chloromercurlbenzoate, respectively. The enzyme activity was inactivated about 75% by 1mM of o-phenanthrotine and monoiodoacetate. But the enzyme activity was stimulated up to 200%s by 1mM of 2-mercaptoethanol.
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KEYWORD
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