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KMID : 0364819880260030207
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Korean Journal of Microbiology
1988 Volume.26 No. 3 p.207 ~ p.214
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Characterization of Cytoslne Deaminase with Substrate Specificity to 5-Fluorocytosine
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Yeehn Yeeh
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Abstract
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1
A cytodne deamiaase from the cell-free extract of an isolate was examined after ethyl alcohol fractoaafba. The enzyme catalyzed the conversion of 5-fluorocyloslae to 5-flooroarat0 by the poaadoa of spedfldty to the substrate. The optimum temperature and storage time on the stabtty of
the enzyme were at below 50°C and near 2 days In tris-Hⓒ buffer. The ma:dmam activity was she
presented at 9.0 In pH and 45°C is temperature. The pHs and temperatures for the enzyme activity ranged from i.5-9.5 and from 40-50°C, respectively. The presence of Ag+, Hg2+, or Zn2+ in the reac
tion mixture molted In the marked inhibition t? the activity, but 1 mM of Fey+, K+; or Na+ increased the enzyme activity. The enzyme preparation was aot affected by inhibitors used except N-etbyim:ielmide of I and 10 mM, and considerably activated by 1 mM of pyrophosphate and 10 mM of phosphate.
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