KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics and thermodynamics, overview | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Pseudomonas aeruginosa | - |
gene pchB | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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) | Pseudomonas aeruginosa | |
isochorismate = salicylate + pyruvate | kinetic mechanism and transition state of the elimination reaction, overview | Pseudomonas aeruginosa |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
isochorismate | isochorismate undergoes elimination to form salicylate and pyruvate and rearrangement to form isoprephenate in the absence of enzyme | Pseudomonas aeruginosa | salicylate + pyruvate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IPL | - |
Pseudomonas aeruginosa |
isochorismate-pyruvate lyase | - |
Pseudomonas aeruginosa |
PchB | - |
Pseudomonas aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas aeruginosa |