2.7.4.13 D16N site-directed mutagenesis of the P loop-related residue, the mutant shows reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 D170N site-directed mutagenesis of the core residue, almost inactive mutant 739645 2.7.4.13 E176Q site-directed mutagenesis of the core residue, almost inactive mutant 739645 2.7.4.13 G137A site-directed mutagenesis of the dNMP-binding residue, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 K131E site-directed mutagenesis, of the dNMP-binding residue, the mutant shows slightly increased activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 additional information all enzyme mutants but T17S show an increased pH optimum compared to the wild-type enzyme 739645 2.7.4.13 Q134A site-directed mutagenesis of the dNMP-binding residue, the mutant shows reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 R130K site-directed mutagenesis of the dNMP-binding residue, almost inactive mutant 739645 2.7.4.13 R172I site-directed mutagenesis of the core residue, almost inactive mutant 739645 2.7.4.13 S13A site-directed mutagenesis of the P loop-related residue, the mutant shows reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 T138A site-directed mutagenesis of the dNMP-binding residue, the mutant shows reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 T17N site-directed mutagenesis of the P loop-related residue, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type enzyme 739645 2.7.4.13 T17S site-directed mutagenesis, of the P loop-related residue, the mutant shows reduced activity compared to the wild-type enzyme 739645 2.7.4.13 W150A site-directed mutagenesis of the core residue 739645 2.7.4.13 W150F site-directed mutagenesis of the conserved residue, the mutant shows unaltered activity compared to the wild-type enzyme 739645