Literature summary for 5.4.99.5 extracted from

Ishida, T.; Fedorov, D.G.; Kitaura, K.
All electron quantum chemical calculation of the entire enzyme system confirms a collective catalytic device in the chorismate mutase reaction (2006), J. Phys. Chem. B, 110, 1457-1463.

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Activating Compound

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

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Chorismate	Bacillus subtilis	-	Prephenate	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P19080	-	-

Reaction

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	a

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms	Comment	Organism
Bacillus subtilis chorismate mutase	-	Bacillus subtilis
BsCM	-	Bacillus subtilis

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)