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- W1514331378 abstract "Abstract The deoxythymidylate phosphohydrolase (dTMPase) induced by Bacillus subtilis bacteriophage PBS2 (whose DNA contains uracil instead of thymine) has been partially purified and shown to possess deoxyuridylate phosphohydrolase (dUMPase) activity. The similarities of induction period, pH dependence, heat and trypsin inactivation, sulfhydryl reagent and fluoride inhibition, metal ion effects, kinetic constants for substrates and products, and apparent molecular weight suggest that a single enzyme catalyzes both dTMPase and dUMPase reactions. Although the PBS2 phosphohydrolase is active on many different deoxyribonucleotide derivatives of 4-hydroxypyrimidine and 6-hydroxypurine, it displays a strong preference for dTMP (apparent Km of 10-5 m versus 10-3 m for dUMP). This phage-induced phosphohydrolase may be responsible for the exclusion of thymine from PBS2 DNA during PBS2 phage infection, by eliminating the substrate (dUMP) and the product (dTMP) of the B. subtilis thymidylate synthetase." @default.
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- W1514331378 date "1973-02-01" @default.
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- W1514331378 title "Deoxythymidylate Phosphohydrolase Induced by Bacteriophage PBS2 during Infection of Bacillus subtilis" @default.
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- W1514331378 doi "https://doi.org/10.1016/s0021-9258(19)44309-3" @default.
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