Abstract
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) of uracil in DNA arising either by incorporation during DNA synthesis or by deamination of cytosine in DNA.
Original language | English (US) |
---|---|
Pages (from-to) | 3194-3201 |
Number of pages | 8 |
Journal | Biochemistry |
Volume | 16 |
Issue number | 14 |
DOIs | |
State | Published - Jul 1 1977 |
ASJC Scopus subject areas
- Biochemistry