Partial purification and characterization of a uracil DNA N-glycosidase from Bacillus subtilis

Journal Article · Tue Jul 12 04:00:00 EDT 1977 · Biochemistry; (United States)

OSTI ID:7302947

Cone, R; Duncan, J; Hamilton, L; Friedberg, E C

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 CO/sup 2 +/, Fe/sup 2 +/, or Zn/sup 2 +/. 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)/sub 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.

• Research Organization: Stanford Univ., CA
• OSTI ID: 7302947
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 16:14; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AZINES
BACILLUS
BACILLUS SUBTILIS
BACTERIA
BIOLOGICAL RECOVERY
BIOLOGICAL REPAIR
CHEMICAL PROPERTIES
DNA
ENZYMES
HETEROCYCLIC COMPOUNDS
HYDROLASES
HYDROXY COMPOUNDS
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PURIFICATION
PYRIMIDINES
RECOVERY
REPAIR
URACILS