EC Number   |
General Information |
Reference |
|---|
   4.2.99.21 | evolution |
PchB is a structural homologue of the AroQ chorismate mutases |
726963 |
| 4.2.99.21 | metabolism |
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 |
-, 748448 |
| 4.2.99.21 | metabolism |
the enzyme is involved in siderophore pyochelin via salicylate biosynthesis |
726963 |
| 4.2.99.21 | metabolism |
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). Salicylate synthase converts chorismate into salicylate through a two-step reaction |
-, 747617 |
| 4.2.99.21 | metabolism |
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). 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 |
-, 747617 |
| 4.2.99.21 | more |
structure-function relationship, biocatalysis of pericyclic reactions, overview. For PchB, the pericyclic reaction is a concerted but asynchronous [1,5]-sigmatropic shift with a quantitative transfer of hydrogen from C2 to C9. Major structural difference between the apo form and the pyruvate-bound or the pyruvate-and salicylate-bound forms of PchB: the active site loop between helix 1 and helix 2 is disordered in the apo structure but fully ordered in the ligand-bound structures. The difference between the open and closed structures is due to a conserved active site lysine 42, which hydrogen bonds to a bound pyruvate molecule. Quantum mechanical/molecular mechanical molecular dynamics simulations, overview |
726963 |
| 4.2.99.21 | physiological function |
involved in the biosynthesis of the siderophore yersiniabactin |
708916 |
| 4.2.99.21 | physiological function |
mycobactins are small-molecule iron chelators (siderophores) produced by Mycobacterium tuberculosis (Mtb) for iron mobilization. Siderophores are small-molecule iron chelators that scavenge iron from host tissues and uptake of heme through a specialized heme receptor followed by heme degradation to release the iron. The bifunctional salicylate synthase MbtI catalyzes the first step of mycobactin biosynthesis through the conversion of the primary metabolite chorismate into salicylic acid via isochorismate |
-, 748448 |
| 4.2.99.21 | physiological function |
salicylic acid (SA) is an essential hormone for development and induced defense against biotrophic pathogens in plants. The formation of SA mainly derives from chorismate via isochorismate synthase (ICS, EC 5.4.4.2) and isochorismate pyruvate lyase (IPL, EC 4.2.99.21)-mediated steps in Arabidopsis thaliana |
-, 748659 |
| 4.2.99.21 | physiological function |
the enzyme is involved in the biosynthesis of pyochelin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria |
-, 747617 |
