Literature summary extracted from
Carrell, C.J.; Bush, L.A.; Mathews, F.S.; Di Cera, E.
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
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.4.21.5 |
vitamin K |
dependent on |
Homo sapiens |
|
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.21.5 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.21.5 |
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]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
3.4.21.5 |
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
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.4.21.5 |
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 |
|
3.4.21.5 |
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 |
|
3.4.21.5 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.5 |
Homo sapiens |
- |
- |
- |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.4.21.5 |
25 |
- |
assay at |
Homo sapiens |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.21.5 |
8 |
- |
assay at |
Homo sapiens |