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 |