Bacteriophage PBS2-induced deoxycytidine triphosphate deaminase in Bacillus subtilis.
The dCTP deaminase induced by Bacillus 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.
D000619:Aminohydrolases / Q000096:biosynthesis*; D001412:Bacillus subtilis; D001435:Bacteriophages / Q000032:analysis / Q000201:enzymology* / Q000378:metabolism; D002474:Cell-Free System; D002701:Chloramphenicol / Q000494:pharmacology; D002854:Chromatography, Paper; D004267:DNA Viruses; D004279:DNA, Viral / Q000032:analysis / Q000096:biosynthesis; D003609:Dactinomycin / Q000494:pharmacology; D003841:Deoxycytidine; D004790:Enzyme Induction; D009154:Mutation; D009709:Nucleotide Deaminases / Q000096:biosynthesis* / Q000378:metabolism; D012293:Rifampin / Q000494:pharmacology; D013941:Thymine / Q000032:analysis; D014316:Tritium; D014498:Uracil / Q000032:analysis
D004279:DNA, Viral; D003841:Deoxycytidine; D014316:Tritium; D003609:Dactinomycin; D014498:Uracil; D002701:Chloramphenicol; D000619:Aminohydrolases; D009709:Nucleotide Deaminases; D013941:Thymine; D012293:Rifampin