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Chemical midification of Cytosine Deaminase from Aspergillus fumigatus
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Chemical midification of Cytosine Deaminase from Aspergillus fumigatus
Yu, Tae Shick , Kim, Jung , Kim, Hyun Soo
Journal of Microbiology 1998;36(1):39-42

Department of Microbiology, College of Natural Science, Keimyung UniversityDepartment of Microbiology, College of Natural Science, Keimyung University
Corresponding author:  Yu, Tae Shick ,
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Essential amino acids involved in the catalytic mechanisms of cytosine deaminase from Aspergillus fumigatus IFO 5840 were determined by chemical modification studies. The enzyme was perfectly inhibited by N-bromosuccinimide, chloramines-T, pyridoxal-5’-phosphate, and p-chloromercuribenzoate. It was strongly inhibited by phenylmethyl sulfonyl fluoride, and weakly inhibited by phenylglyoxal. The inactivation of the enzyme activity by p-CMB was reversed by sulfhydryl reagents. Furthermore, activities inhibited by chloramines-T, pyridoxal-5’-phosphate, results, we speculate that tryptophan, methionine, lysine and cysteine residues are located in ornear the active center of the cytosine deaminase, while a serine is indirectly involved I the enzyme activity.

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    Chemical midification of Cytosine Deaminase from Aspergillus fumigatus
    J. Microbiol. 1998;36(1):39-42.
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