[51] Cytosine and cytidine deaminase from yeast

@article{Ipata197851CA,
  title={[51] Cytosine and cytidine deaminase from yeast},
  author={P. Ipata and G. Cercignani},
  journal={Methods in Enzymology},
  year={1978},
  volume={51},
  pages={394-401}
}
Publisher Summary This chapter describes the purification procedure of cytosine and cytidine deaminase from yeast. The hydrolytic deamination of cytidine to uridine and of cytosine to uracil is catalyzed in yeast by two distinct enzyme proteins. Both cytosine and cytidine deaminase activities can be determined by direct spectrophotometric assay from the fall in absorbance at 286 nm following the conversion of the 4-amino to the 4-keto compounds. The pooled active fractions can be stored at -20… Expand
Cloning, overexpression, and purification of cytosine deaminase from Saccharomyces cerevisiae.
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A purification protocol has been developed which permits recovery of 60% of cytosine deaminase in active form from induced cell lysates after two purification steps, which will be useful for isolating large quantities of pure enzyme which are required for the preclinical evaluation of monoclonal antibody-cytosineDeaminase conjugates in combination with 5-fluorocytosines. Expand
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Selenomethionine-containing protein has been prepared and crystallized for MAD phasing and allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. Expand
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Evidence is provided that the pyrimidine nucleoside phosphorylases were a single enzyme capable of utilizing uridine, deoxyuridine and thymidine (and corresponding bases) as substrates and can be viewed as potential targets at which to direct chemotherapeutic agents. Expand
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T. vaginalis has no appreciable dihydrofolate reductase or thymidylate synthetase; it grows normally in millimolar concentrations of methotrexate, pyrimethamine, or trimethoprim, and cannot incorporate labels from exogenous uracil or uridine into DNA, but has an enzyme thymidine phosphotransferase in the sedimentable fraction which converts thymazine to TMP. Expand
Crystal Structure of Yeast Cytosine Deaminase
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The enzyme shares similar active-site architecture to cytidine deaminases and an unusually high structural homology to 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase and thereby may define a new superfamily. Expand
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An enzyme 5-methyldeoxycytidylate aminohydrolase, responsible for this conversion, was detected in a cell-free system of Xp12-infected cells and seems likely that the conversion occurred at the nucleotide level of 5-methylcytosine. Expand
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A deoxycytidine deaminase that was extremely thermostable in the presence of dithiothreitol was found in a mesophilic bacterium isolated from soil and greatly stabilized the enzyme. Expand
Expulsion of uracil and thymine from the yeast Saccharomyces cerevisiae: contrasting responses to changes in the proton electrochemical gradient.
  • A. Eddy
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  • 1997
TLDR
It was concluded that uracil exit is probably not driven by the proton gradient but may utilize ATP directly, and thymine uptake from the medium only occurred when delta mu H+ was dissipated, either by DNP or azide, or by manipulation of the external ionic environment. Expand
Evidence of a new phosphoryl transfer system in nucleotide metabolism
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The proposed mechanism suggests a physiological role for the enzymes and for the AMP–AMP phosphotransferase reaction under conditions of extreme energy drain (such as hypoxia or temporary anoxia, as in cancer tissues) when the enzymes cannot display their conventional activity because of substrate deficiency. Expand
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