3.2.2.23	A288V	naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1, activity, substrate specificity and kinetics compared to the wild-type enzyme, overview	708484	
3.2.2.23	D322N	naturally occuring polymorphism, the mutant is 2.3fold more specific for the correct opposite base than the wild-type enzyme, activity, substrate specificity and kinetics compared to the wild-type enzyme	708484	
3.2.2.23	E131R	loss of activity	750392	
3.2.2.23	E173Q	no enzymic activity, E173 may play a crucial role in forming the active site pocket	667594	
3.2.2.23	E2Q	no enzymic activity, interactions with G167 and Y170 are interupted	667594	
3.2.2.23	E3Q	crystallization data	680361	
3.2.2.23	E3Q	inactive. Mutant binds DNA duplexes containing spiroiminodihydantoin or guanidinohydantoin about 1000fold more tightly over corresponding duplexes containing 8-oxoguanine	678318	
3.2.2.23	E77S	in wild-type, 8-oxoguanine is bound via E77 in syn conformation. In mutant E77S, which reflects the sequence of the Escherichia coli enzyme, 8-oxoguanine is preferentially bound in the anti conformation	678139	
3.2.2.23	F110A	the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps	710030	
3.2.2.23	F110W	the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps	710030