Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
R90K | The ES, TS, and product structures of the mutants are determined based on the wild-type structure. The hydrogen-bond lengths of the mutants differ from the wild-type. The two mutants chemical reaction progresses in a similar way. No large geometrical changes in and around the active site along the reaction path: only a small rearrangement of the hydrogen-bond sites. As for Lys90/Cit90 mutant reactions, no large conformational change is observed in the overall protein structure except for the geometries around the mutation point. Although the catalytic activity of R90K is inferior to that of the wild-type, the enzymatic mechanism of the R90K mutant is similar to the wild-type. The main anticatalytic factor of R90Cit mutant is the ES stabilization as a result of destabilizing the substrate by the surrounding electrostatic field because of the mutated enzyme. Therefore the TS stabilization mechanism of the Cit90 mutant is quite different from that of the wild-type BsCM | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | Bacillus subtilis | - |
Prephenate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P19080 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Chorismate = prephenate | Wild-type-reaction: Arg63, Arg116, Arg7, and Tyr108 required for the relative orientation of the substrate at the active site, the structural rearrangement in the Glu78-Arg90-substrate controls the strength of the hydrogen bonds. The hydrogen bonds connecting the Glu78-Arg90-substrate cooperatively control the stability of TS relative to the ES complex and the positive charge on Arg90 polarizes the substrate in the TS region to gain more electrostatic stabilization. Method: electron quantum chemical calculations by fragment molecular orbital (FMO) method. The structural refinement and reaction path search are performed by the ab initio QM/MM treatment. Usage of the AMBER standard parameter set (parm.96) for the MM force-field calculations. Reaction path search: On the basis of the gas-phase IRC (intrinsic reaction coordinate) profile of chorismate isomerization, the linear reaction path is calculated first | Bacillus subtilis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
Activation Energies in the enzyme reactions by AMBER and FMO calculations for wild-type and mutants are shown. These results are potential energy, not free energy | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | - |
Bacillus subtilis | Prephenate | - |
? | |
additional information | The enzymatic reaction is considered to proceed via a pericyclic transition state | Bacillus subtilis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Bacillus subtilis chorismate mutase | - |
Bacillus subtilis |
BsCM | - |
Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained | Bacillus subtilis |