Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex pyrophilus | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
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. | Aquifex pyrophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | - |
Aquifex pyrophilus | D-glutamate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
glutamate racemase | - |
Aquifex pyrophilus |
MurI | - |
Aquifex pyrophilus |