4.2.99.B1	D256A	site-directed mutagenesis, C-terminal polymerase domain, completely eliminates dRP lyase activity, proficient in DNA synthesis by the polymerase reaction	694332	
4.2.99.B1	D829N/E830Q	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	E71Q	retains wild-type enzyme activity	692940	
4.2.99.B1	E75A	about 75% of wild-type enzyme activity	692940	
4.2.99.B1	F25W	about 85% of wild-type enzyme activity	692940	
4.2.99.B1	H34G	about 45% of wild-type enzyme activity	692940	
4.2.99.B1	K310A	eliminates more than 90% of the wild-type dRP lyase activity, indicating that Lys 310 is the main nucleophile involved in the reaction, forming the Schiff base internediate during beta-elimination	692957	
4.2.99.B1	K35A	about 50% of wild-type enzyme activity, Lys72 and Lys35 are involved in the dRP lyase reaction catalyzed by the 8-kDa domain and Lys35 is involved in 5'-phosphate recognition. Lys35 may stabilize the leaving group in the dRP lyase reaction through its interaction with the 5'-phosphate of the DNA-terminus	692940	
4.2.99.B1	K35A	part of the active site, 50% loss of enzyme activity	692010	
4.2.99.B1	K35A/K68A	part of the active site, similar to wild-type enzyme activity	692010