Partial purification and characterization of a uracil DNA N-glycosidase from Bacillus subtilis.
Copyright policy )Partial purification and characterization of a uracil DNA N-glycosidase from Bacillus subtilis.
A uracil specific DNA N-glycosidase activity has been partially purified from crude extracts of Bacillus subtilis. The enzyme has a molecular weight of approximately 24 000 with no subunit structure. It has no requirement for any known cofactors but is inhibited in the presence of Co2+, Fe2+, or Zn2+. The enzyme is specific for uracil in single- and double-stranded deoxyribonucleopolymers and does not release free uracil from RNA or from poly(rU):poly(dA). In addition, neither Udr, dUMP, nor dUTP is recognized as substrate. The enzyme will attack small poly(dU) oligomers but the minimum size recognized as substrate is (pU)4. This enzyme may have a role in the repair (by base excision) or uracil in DNA arising either by incorporation during DNA synthesis or by deamination of cytosine in DNA.
Poly U, Iron, Cobalt, DNA, Molecular Weight, Kinetics, Structure-Activity Relationship, Zinc, Polydeoxyribonucleotides, Oligodeoxyribonucleotides, Uracil, N-Glycosyl Hydrolases, Bacillus subtilis
Poly U, Iron, Cobalt, DNA, Molecular Weight, Kinetics, Structure-Activity Relationship, Zinc, Polydeoxyribonucleotides, Oligodeoxyribonucleotides, Uracil, N-Glycosyl Hydrolases, Bacillus subtilis
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