EC Number   |
General Information |
Reference |
|---|
    5.1.2.2 | evolution |
mandelate racemase is a member of the enolase superfamily. The ability of the enzyme to form and deprotonate a Schiff-base intermediate furnishes a mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor |
747083 |
| 5.1.2.2 | more |
development and evaluation of a virtual mutant screening method based on the binding energy in the transition state, the method is beneficial in enzyme rational redesign and helps to better understand the catalytic properties of the enzyme, and it is effective in predicting the trend of mutational effects on catalysis, molecular dynamic simulation, overview |
727384 |
| 5.1.2.2 | more |
enzyme molecular dynamics simulation and molecular docking |
-, 746856 |
| 5.1.2.2 | more |
role for the Broensted acid-base catalysts of mandelate racemase in transition state stabilization. Enzyme-catalyzed abstraction of an alpha-proton from a carbon acid substrate with a high pKa. Residues Lys166 and His297 play dual roles in catalysis: they act as Broensted acid-base catalysts, and they stabilize both the enolate moiety and phenyl ring of the altered substrate in the transition state |
747095 |
| 5.1.2.2 | more |
significance of Ser139 in mandelate racemization, the active site residue S139 forms a hydrogen bond with one carboxyl oxygen of the substrate mandelate, residues S139 and E317 of mandelate racemase have a synergistic effect on transition state stabilization, overview |
728000 |
| 5.1.2.2 | more |
the enzyme's 20s loop likely undergoes a significant conformational change upon binding (R)-mandelate |
727042 |
| 5.1.2.2 | more |
the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C |
742923 |
| 5.1.2.2 | physiological function |
enzyme catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate |
706599 |
| 5.1.2.2 | physiological function |
mandelate racemase catalyzes the interconversion of the enantiomers of mandelate |
747095 |
