EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.21.6 | additional information | - |
additional information | kinetics of FVIIIa inactivation | Homo sapiens | |
3.4.21.69 | additional information | - |
additional information | kinetics | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.69 | Ca2+ | - |
Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.6 | activated factor VIII + H2O | Homo sapiens | proteolytic inactivation | factor VIII | - |
? | |
3.4.21.6 | factor VIII + H2O | Homo sapiens | proteolytic activation by removal of the B domain | activated factor VIII + B domain | - |
? | |
3.4.21.69 | active factor Va + H2O | Homo sapiens | proteolytic inactivation of the cofactor in the prothrombinase complex | inactive factor V + ? | - |
? | |
3.4.21.69 | active factor VIII + H2O | Homo sapiens | activated protein C and activated factor X play a role in proteolytic inactivation of activated coagulation factor VIII involving the B domain, the inactivated substrate factor VIII is less efficient on blood clotting, overview | inactive factor VIII + domain B | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.6 | Homo sapiens | - |
- |
- |
3.4.21.69 | Homo sapiens | - |
- |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.4.21.69 | additional information | - |
- |
Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.6 | activated factor VIII + H2O | proteolytic inactivation | Homo sapiens | factor VIII | - |
? | |
3.4.21.6 | activated factor VIII + H2O | inactivation by cleavage at Arg336 and Lys36 of domain A1, low activity | Homo sapiens | factor VIII | - |
? | |
3.4.21.6 | factor VIII + H2O | proteolytic activation by removal of the B domain | Homo sapiens | activated factor VIII + B domain | - |
? | |
3.4.21.6 | factor VIII + H2O | activation by cleavage at Arg1689 and Arg1721 of domain A3 | Homo sapiens | activated factor VIII + B domain | - |
? | |
3.4.21.69 | active factor Va + H2O | proteolytic inactivation | Homo sapiens | inactive factor V + ? | - |
? | |
3.4.21.69 | active factor Va + H2O | proteolytic inactivation of the cofactor in the prothrombinase complex | Homo sapiens | inactive factor V + ? | - |
? | |
3.4.21.69 | active factor VIII + H2O | activated protein C and activated factor X play a role in proteolytic inactivation of activated coagulation factor VIII involving the B domain, the inactivated substrate factor VIII is less efficient on blood clotting, overview | Homo sapiens | inactive factor VIII + domain B | - |
? | |
3.4.21.69 | active factor VIIIa + H2O | proteolytic inactivation, cleavage at Arg336 and Arg572 in domains A1 and A2, respectively | Homo sapiens | inactive factor VIII + domain B | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.6 | activated factor X | - |
Homo sapiens |
3.4.21.6 | FXa | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.21.69 | 37 | - |
assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.21.69 | 7.2 | - |
assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.69 | protein S | complexed witht the activated protein C, increases the activity 6-10fold | Homo sapiens |