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Literature summary extracted from
- Wild-type and molten globular chorismate mutase achieve comparable catalytic rates using very different enthalpy/entropy compensations (2014), Sci. China Chem., 57, 156-164 .
No PubMed abstract available
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | Meloidogyne javanica | - |
Prephenate | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.5 | Meloidogyne javanica | Q9XTN9 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.5 | Chorismate = prephenate | catalytic reaction mechanism, role of conformational dynamics and entropies in enzyme catalysis, overview. Large-scale conformational dynamics make important catalytic contributions to sampling conformational regions in favor of binding the transition state of substrate | Meloidogyne javanica |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | - |
Meloidogyne javanica | Prephenate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | MjCM | - |
Meloidogyne javanica |
| 5.4.99.5 | NC30 | - |
Meloidogyne javanica |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | evolution | primitive molten globular enzymes might, like mMjCM, have had substantial advantages in forming stronger transition state interactions, since they could be more effective to explore different conformational states favorable to tighter binding of transition state | Meloidogyne javanica |
| 5.4.99.5 | additional information | wild-type and molten globular chorismate mutase achieve comparable catalytic rates using very different enthalpy/entropy compensations, analysis using ab initio quantum mechanical/molecular mechanical minimum free-energy path method, overview. Site-specific, non-uniform rigidity changes of the enzymes during catalysis. The change of conformational entropy from the ground state to the transition state revealed distinctly contrasting entropy/enthalpy compensations in the dimeric wild-type enzyme and its molten globular monomeric variant. Molecular dynamics simulations | Meloidogyne javanica |
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