EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.21 | additional information | enzyme activation involves residue 343, mechanisms, overview | Homo sapiens | |
3.4.21.21 | tissue factor TF | TF-induced allosteric activation of FVIIa, binding structure, overview | Homo sapiens | |
3.4.21.21 | vitamin K | dependent on | Homo sapiens |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.4.21.21 | medicine | recombinant FVIIa constitutes an efficient substitution therapy for treatment of patients with haemophilia A and haemophilia B which lack or have dysfunctional FVIII and FIX, respectively, pharmacological mechanism of action of FVIIa, overview | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.21.21 | K337A | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Homo sapiens |
3.4.21.21 | additional information | construction of FVIIa analogues with a stabilized activation domain and N-terminal insertion | Homo sapiens |
3.4.21.21 | P10Q | site-directed mutagenesis, the mutant shows 2fold enhancement in membrane binding affinity over wild-type FVIIa | Homo sapiens |
3.4.21.21 | P10Q/K32E | site-directed mutagenesis, the mutant shows 27fold enhancement in membrane binding affinity over wild-type FVIIa, the double mutant displays a significantly improved procoagulant effect in haemophilic blood | Homo sapiens |
3.4.21.21 | P10Q/K32E/D33F/A34E | site-directed mutagenesis, the mutant shows 150-300fold enhancement in membrane binding affinity over wild-type FVIIa | Homo sapiens |
3.4.21.21 | V158D/E296V/M298Q | site-directed mutagenesis, FVIIa analogues with a stabilized activation domain and N-terminal insertion, the mutant shows increased activity compared to the wild-type enzyme | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.21.21 | extracellular | - |
Homo sapiens | - |
- |
3.4.21.21 | membrane | the major function of the enzyme's Gla domain is to attach FVIIa to membranes, i.e. to add binding energy to the interaction with membrane-associated tissue factor | Homo sapiens | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.21 | Ca2+ | activates | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.21 | factor IX + H2O | Homo sapiens | - |
factor IXa + ? | - |
? | |
3.4.21.21 | Factor X + H2O | Homo sapiens | - |
Factor Xa + ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.21 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.21.21 | proteolytic modification | zymogen FVII is converted to the activated form by proteolytic cleavage of the Arg152{15}-Ile153{16} peptide bond, zymogen factor VII is activated by thrombin | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.21 | factor IX + H2O | - |
Homo sapiens | factor IXa + ? | - |
? | |
3.4.21.21 | Factor X + H2O | - |
Homo sapiens | Factor Xa + ? | - |
? | |
3.4.21.21 | additional information | structure-function relationship, the enzyme forms a complex with the cell surface receptor tissue factor TF required for attaining its catalytically competent conformation, Asp338 is a catalytically important residue | Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.21.21 | More | structure-function relationship, overview | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.21 | FVIIa | - |
Homo sapiens |
3.4.21.21 | More | the enzyme is a member of the trypsin family of serine proteases | Homo sapiens |