EC Number   |
Reaction |
Reference |
|---|
   4.2.99.21 | isochorismate = salicylate + pyruvate |
- |
- |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
a reactive substrate conformation is formed upon loop closure of the active site and ordering of the loop contributes to the entropic penalty for converting the enzyme substrate complex to the transition state. The thermodynamic parameters of the physiological lyase activity of PchB show that the reaction is clearly enthalpically driven, and has a very large entropic penalty of 24.3 cal/(mol K), which is more than 1.5-fold greater than that of the uncatalyzed reaction of 15.77 cal/(mol K) |
715303 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
kinetic mechanism and transition state of the elimination reaction, overview |
715303 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate |
-, 747617 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate. In the second reaction, pyruvate is eliminated through an intramolecular [3,3]-sigmatropic rearrangement, formerly a retro-Ene reaction, to afford salicylic acid via bicyclic transition state TS2 |
-, 748448 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
reaction mechanism with catalytic residue Lys42, modeling, overview |
726963 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
reaction mechanism, the IPL reaction is a concerted but asynchronous hydrogen transfer, by a proposed [1,5]-sigmatropic reaction mechanism with a pericyclic transition state, quantum mechanical/molecular-mechanical calculations and simulations, overview |
728765 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
the enzyme achieves catalysis of both pericyclic reactions, isochorismate-pyruvate lyase and chorismate-pyruvate lyase, EC 4.1.3.40, in part by the stabilization of reactive conformations and in part by electrostatic transition-state stabilization. Both, substrate organization and electrostatic transition state stabilization, contribute to catalysis |
714268 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
the lysine42 residue is required in a specific conformation to stabilize the transition state |
729222 |
| 4.2.99.21 | isochorismate = salicylate + pyruvate |
[1,5]-sigmatropic reaction mechanism that invokes electrostatic catalysis in analogy to the [3,3]-pericyclic rearrangement of chorismate in chorismate mutase |
669382 |
