EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   4.2.99.21 | more |
enzyme additionally catalyzes the rearrangement of chorismate into prephenate and shows chorismate mutase activity. Both transformation of isochorismate into pyruvate and salicylate and the rearrangement of chorismate into prephenate proceed via a pericyclic reaction mechanism |
Pseudomonas aeruginosa |
? |
- |
? |
| 4.2.99.21 | more |
enzyme converts chorismate to salicylate. The reaction proceeds through the intermediate isochorismate |
Yersinia enterocolitica |
? |
- |
? |
| 4.2.99.21 | more |
enzyme directly converts chorismat into salicylate |
Yersinia enterocolitica |
? |
- |
? |
| 4.2.99.21 | more |
isochorismate is a kinetically competent intermediate in the synthesis of salicylate from chorismate. At pH values below 7.5 isochorismate is the dominant product while above this pH value the enzyme converts chorismate to salicylate without the accumulation of isochorismate in solution. MbtI may exploit a sigmatropic pyruvate elimination mechanism |
Mycobacterium tuberculosis |
? |
- |
? |
| 4.2.99.21 | more |
nucleophilic substitution reaction, enzyme is able to use H2O as a nucleophile. Catalytic base K147 is not solely responsible for activation of H2O as a nucleophile |
Escherichia coli |
? |
- |
? |
| 4.2.99.21 | more |
the 2H kinetic isotope effects on kcat and the ratio kcat/Km are 2.34 and 1.75, respectively. Chemistry is significantly rate-determining for the enzyme. The magnitude of the isotope effect is consistent with considerable C-H bond cleavage in the transition state. The significant 2H kinetic isotope effect and quantitative transfer of the label to pyruvate are both consistent with a pericyclic reaction mechanism |
Pseudomonas aeruginosa |
? |
- |
? |
| 4.2.99.21 | more |
PchB can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency |
Pseudomonas aeruginosa |
? |
- |
? |
| 4.2.99.21 | more |
PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency |
Pseudomonas aeruginosa |
? |
- |
? |
| 4.2.99.21 | more |
PchB possesses weak chorismate mutase activity as well and is able to catalyze two distinct pericyclic reactions in a single active site. The enzyme tends to bring its non-native substrate in the same conformation as its native substrate |
Pseudomonas aeruginosa |
? |
- |
? |
| 4.2.99.21 | more |
isochorismate synthase PhA additionally shows isochorismate lyase activity. Site-specific mutation of active site residues promotes lyase activity |
Pseudomonas aeruginosa |
? |
- |
? |
