EC Number   |
Subunits |
Reference |
|---|
   4.2.99.B1 | monomer |
1 * 39000, consists of a 31 kDa C-terminal and a 8 kDa amino-terminal domain |
692941 |
| 4.2.99.B1 | monomer |
1 * 45000, SDS-PAGE, wild-type mitochondrial pol beta and K72A mutant |
692962 |
| 4.2.99.B1 | More |
alignment with the rat nuclear enzyme shows that the mitochondrial pol beta contains the essential conserved amino acids Lys35, Lys60, Lys68, and Lys72 |
692962 |
| 4.2.99.B1 | More |
dRP lyase activity is intrinsic to the catalytic subunit of human pol gamma |
694925 |
| 4.2.99.B1 | More |
polymerase theta is a ca. 300 kDa polypetide. The 98-kDa C-terminal region possesses both the DNA polymerase and the dRP lyase activity. The 5'-dRP lyase activity is independent of the polymerase activity. The polymerase inactive mutant D829N/E830Q retains full 5'-dRP lyase activity. Domain mapping of the 98-kDa enzyme reveals that the 5'-dRP lyase active site resides in a 24-kDa-domain |
694467 |
| 4.2.99.B1 | More |
Rev1 domain mapping of the C-terminal domain by limited proteolysis |
748781 |
| 4.2.99.B1 | More |
the 8-kDa domain of polymerase beta is responsible for single-stranded DNA binding, 5'-phosphate recognition, and dRP lyase activity, formed by the amino acid residues 1-91 of Li Polbeta. The residues Tyr39, Lys60, Lys68, Lys72, Glu75, and Glu84 play a role in the catalysis. Lys72, identified as the nucleophile in Polbeta is responsible for Schiff base forming during beta-elimination of the dRP moiety |
692012 |
| 4.2.99.B1 | More |
the catalytic subunit of the HSV-1 DNA polymerase exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities |
694866 |
