A model for enzyme-substrate interaction in alanine racemase.

摘要: We report on a theoretical model for the complex of enzyme alanine racemase with its natural substrate (l-alanine) and cofactor (pyridoxal 5‘-phosphate). Electrostatic potentials were calculated ionization states predicted all ionizable groups in racemase. Some rather unusual charge certain residues. Tyr265‘ has an unusually low pKa 7.9 at pH 7.0 average −0.37, meaning that 37% residues ensemble molecules are phenolate form. At 8−9, majority side will be This lends support to experimental evidence is catalytic base involved conversion l-alanine d-alanine. Residues Lys39 Lys129 have charges +0.91 +0.14, respectively, 7.0. believed d-alanine l-alanine, present results show that, least so...