EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
    5.1.1.3 | -999 |
- |
- |
2095 |
| 5.1.1.3 | -999 |
- |
computer simulations on a QM/MM (quantum mechanics/molecular mechanics) potential energy surface are carried out to gain insights into the catalytic mechanism of glutamate racemase (MurI). Results suggest at least two possible roles for MurI as a catalyst: (1) to activate the bound substrate by donating a proton to its carboxylate main chain in a step prior to the racemization process and (2) to optimize the differential stabilization of the intermediate relative to the reactant via an intermolecular effect that comes, partly, from a desolvation effect on the reactant in going from water to the enzyme environment and, partly, from a stabilization effect on the intermediate by the enzymatic residues. Thus, the catalytic effect of glutamate racemase is achieved without resorting to covalent bond formation between the enzyme or cofactor and the transition state. |
675608 |
| 5.1.1.3 | -999 |
- |
Escherichia coli MurI is monomeric in solution and shows extremely low intrinsic activity in either direction (symmetrical kinetic profile), but catalytic turnover is upregulated over 1000fold by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway |
676152 |
| 5.1.1.3 | -999 |
- |
in Bacillus anthracis glutamate racemase is encoded by two genes racE1 and racE2, both enzymes are different in quaternary structure and catalyze the reversible stereoisomerization with similar but not identical kinetic properties |
674336 |
| 5.1.1.3 | -999 |
- |
it is demonstrated that mycobacterial MurI inhibits DNA gyrase activity. Inhibition is not species-specific as Escherichia coli gyrase is also inhibited but is enzyme-specific as topoisomerase I activity remains unaltered. MurI binds to GyrA subunit of the enzyme leading to a decrease in DNA-binding of the holoenzyme. The sequestration of the gyrase by MurI results in inhibition of all reactions catalysed by DNA gyrase. MurI is thus not a typical potent inhibitor of DNA gyrase and instead its role could be in modulation of the gyrase activity |
676216 |
| 5.1.1.3 | -999 |
- |
polarimetric assay method, protocol for measurement of enzyme activity in 96-well microtiter plates |
660705 |
| 5.1.1.3 | 1.53 |
- |
- |
2097 |
| 5.1.1.3 | 2.4 |
- |
purified recombinant enzyme, pH 8.0, 37°C |
749098 |
| 5.1.1.3 | 3 |
- |
37°C |
692381 |
| 5.1.1.3 | 7.7 |
- |
- |
2096 |
