4.2.99.21 isochorismate - Arabidopsis thaliana salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Pseudomonas aeruginosa salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Mycobacterium tuberculosis salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Yersinia pestis salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Yersinia enterocolitica salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate elimination of pyruvate Pseudomonas aeruginosa salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate isochorismate undergoes elimination to form salicylate and pyruvate and rearrangement to form isoprephenate in the absence of enzyme Pseudomonas aeruginosa salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate pericyclic reaction, elimination of pyruvate. The electrostatic field due to PchB at atoms of isochorismate favors the isochorismate to salicylate transition, molecular dynamics simulations, overview Pseudomonas aeruginosa salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Yersinia enterocolitica ATCC 33114 salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Arabidopsis thaliana ecotype Di-17 salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Mycobacterium tuberculosis ATCC 25618 salicylate + pyruvate - ? 412195 4.2.99.21 isochorismate - Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 salicylate + pyruvate - ? 412195 4.2.99.21 additional information 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 ? - ? 89 4.2.99.21 additional information enzyme converts chorismate to salicylate. The reaction proceeds through the intermediate isochorismate Yersinia enterocolitica ? - ? 89 4.2.99.21 additional information enzyme directly converts chorismat into salicylate Yersinia enterocolitica ? - ? 89 4.2.99.21 additional information 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 ? - ? 89 4.2.99.21 additional information 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 ? - ? 89 4.2.99.21 additional information 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 ? - ? 89 4.2.99.21 additional information PchB can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency Pseudomonas aeruginosa ? - ? 89 4.2.99.21 additional information PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency Pseudomonas aeruginosa ? - ? 89 4.2.99.21 additional information 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 ? - ? 89 4.2.99.21 additional information isochorismate synthase PhA additionally shows isochorismate lyase activity. Site-specific mutation of active site residues promotes lyase activity Pseudomonas aeruginosa ? - ? 89 4.2.99.21 additional information salicylate synthase Irp9 additionally shows isochorismate lyase activity Yersinia enterocolitica ? - ? 89 4.2.99.21 additional information incubation of chorismate with the combination of the recombinant proteins EntC (isochorismate synthase, EC 5.4.4.2) and His-PRXR1 results in enhanced levels of salicylate, in a His-PRXR1-dependent manner Arabidopsis thaliana ? - ? 89 4.2.99.21 additional information the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities Yersinia pestis ? - ? 89 4.2.99.21 additional information the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities Yersinia enterocolitica ? - ? 89 4.2.99.21 additional information the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities Mycobacterium tuberculosis ? - ? 89 4.2.99.21 additional information salicylate synthase Irp9 additionally shows isochorismate lyase activity Yersinia enterocolitica ATCC 33114 ? - ? 89 4.2.99.21 additional information incubation of chorismate with the combination of the recombinant proteins EntC (isochorismate synthase, EC 5.4.4.2) and His-PRXR1 results in enhanced levels of salicylate, in a His-PRXR1-dependent manner Arabidopsis thaliana ecotype Di-17 ? - ? 89 4.2.99.21 additional information the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities Mycobacterium tuberculosis ATCC 25618 ? - ? 89