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Literature summary for 3.4.21.5 extracted from
- High resolution crystal structures of free thrombin in the presence of K(+) reveal the molecular basis of monovalent cation selectivity and an inactive slow form (2006), Biophys. Chem., 121, 177-184.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| vitamin K | dependent on | Homo sapiens |  |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| free enzyme mutant R77aA in presence of K+, two molecules in the asymmetric unit, one with the cation site bound to K+ and the other with the site free, X-ray diffraction structure determination and analysis at 1.9 A resolution | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R77aA | the mutant of thrombin prevents the autolytic cleavage at R77a in exosite I and enables crystallization of thrombin free of inhibitors | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | allosteric model based on the kinetic scheme using free enzyme mutant R77aA and the K+ bound F form of the mutant, Michaelis-Menten kinetics, kinetic modeling, overview | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | two ion binding sites per enzyme molecule, binding structure, molecular basis of monovalent cation selectivity, overview, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, overview | Homo sapiens | |
| additional information | the cation-free enzyme form assumes a conformation where the monovalent cation binding site is completely disordered, the S1 pocket is inaccessible to substrate and binding to exosite I is compromised by an unprecedented shift in the position of the autolysis loop | Homo sapiens | |
| Na+ | two ion binding sites per enzyme molecule, free thrombin is a Na+-selective enzyme, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, binding structure, overview | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
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Release 2023.1 (January 2023)
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