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Literature summary for 5.4.99.5 extracted from
- Temperature dependence of the structure of the substrate and active site of the Thermus thermophilus chorismate mutase E x S complex (2006), Biochemistry, 45, 8562-8567.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| The corresponding positional fluctuations from the MD simulation are in good agreement with those obtained by X-ray crystallography | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | Thermus thermophilus | - |
Prephenate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Chorismate = prephenate | Three active sites are formed in the interstices between three subunits. Each active site is composed of the residues of two adjacent subunits. The two Arg hold the chorismate. Crucial distance between Arg6 and Arg63* controls the conformation of the chorismate. The residues in the close vicinity to the chorismate substrate are Arg6, Glu77, Arg89, Tyr 107, Leu114, and Arg115 from one subunit and Phe57*, Ala59*, Arg63*, Leu72*, and Leu73* from the other subunit. The family of the chorismate mutase enzymes shares a common E.S active site | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | - |
Thermus thermophilus | Prephenate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | constisting of three pseudo-alpha/beta barrels | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chorismate mutase | - |
Thermus thermophilus |
| TtCM | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
The average structures of the thermophilic E.S complex at three different temperatures are obtained from the MD simulations. A snapshot of the most important features of the active site of the TtCM E.S complex at 70°C is shown. At this temperature the Boltzmann distribution is primarily composed of reactive conformers - near attack conformers (NACs). The effects of the different temperatures on the distances in the structure are shown. The distances between electrostatic and hydrophobic pairs decrease as temperature decreases | Thermus thermophilus |
| 70 | - |
As the temperature is lowered, distances of electrostatic and hydrophobic interactions decrease. The distance between Glu77-COOH and the hydroxyl oxygen decreases from the optimum | Thermus thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 70 | studies that elucidate the dependence of the E-S active site on temperatures 25, 60 and 70°C | Thermus thermophilus |
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