Bacteriophage PBS2-Induced Deoxycytidine Triphosphate Deaminase in Bacillus subtilis
AUTOR(ES)
Price, Alan R.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=355652Documentos Relacionados
- Bacteriophage PBS2-induced inhibition of uracil-containing DNA degradation.
- Relationship of Bacillus subtilis DNA polymerase III to bacteriophage PBS2-induced DNA polymerase and to the replication of uracil-containing DNA.
- New Deoxyribonucleic Acid Polymerase Induced by Bacillus subtilis Bacteriophage PBS2
- Bacteriophage transformation of PBS2 in Bacillus subtilis.
- Transcriptional specificity of a multisubunit RNA polymerase induced by Bacillus subtilis bacteriophage PBS2.
