Bacteriophage PBS2-Induced Deoxycytidine Triphosphate Deaminase in Bacillus subtilis | Zendy

Alan R. Price | Zendy

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Bacteriophage PBS2-Induced Deoxycytidine Triphosphate Deaminase in Bacillus subtilis

Author(s) -

Alan R. Price

Publication year - 1974

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.14.5.1314-1317.1974

Subject(s) - bacillus subtilis , biology , uracil , thymine , dna , bacteriophage , cytidine deaminase , microbiology and biotechnology , biochemistry , escherichia coli , bacteria , genetics , gene

The dCTP deaminase induced byBacillus subtilis bacteriophage PBS2, whose DNA contains uracil instead of thymine, requires metal ion and thiol activators and has a molecular weight of 125,000. The enzyme displays sigmoidal substrate saturation kinetics and inhibition by dUTP, consistent with the deaminase's proposed role of providing balanced levels of dUTP and dCTP for PBS2 uracil-DNA synthesis.

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