2.7.1.29	D109A	inactive	723640	
2.7.1.29	D109N	inactive	723640	
2.7.1.29	E526K	based on the use of hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, with the QM region described by semiempirical and DFT methods, the reaction mechanism of the wild-type enzyme and the most active experimentally measured mutant (Glu526Lys) with polyphosphate as phosphoryl donor is explored to elucidate the origin of the activity of this mutant. The mutation favors a more adequate position of the polyphosphate in the active site for the following step, the chemical reaction, to take place. Structure-function analysis, overview	759376	
2.7.1.29	E526K	the mutant shows activity with polyphosphate	-, 738418	
2.7.1.29	H128A	inactive	723640	
2.7.1.29	H128K	inactive	723640	
2.7.1.29	H169A	completely inactive	641271	
2.7.1.29	H439A	completely inactive	641271	
2.7.1.29	H56A	the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme	723640	
2.7.1.29	H56N	the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme	723640