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Literature summary for 3.4.21.21 extracted from

  • Olsen, O.H.; Persson, E.
    Cofactor-induced and mutational activity enhancement of coagulation factor VIIa (2008), Cell. Mol. Life Sci., 65, 953-963.
    View publication on PubMed
Search for more literature for 3.4.21.21

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme activation involves residue 343, mechanisms, overview Homo sapiens
tissue factor TF TF-induced allosteric activation of FVIIa, binding structure, overview Homo sapiens
vitamin K dependent on Homo sapiens

Application

Application Comment Organism
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

Protein Variants

Protein Variants Comment Organism
K337A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Homo sapiens
additional information construction of FVIIa analogues with a stabilized activation domain and N-terminal insertion Homo sapiens
P10Q site-directed mutagenesis, the mutant shows 2fold enhancement in membrane binding affinity over wild-type FVIIa Homo sapiens
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
P10Q/K32E/D33F/A34E site-directed mutagenesis, the mutant shows 150-300fold enhancement in membrane binding affinity over wild-type FVIIa Homo sapiens
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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-
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
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor IX + H2O Homo sapiens
-
 factor IXa + ?
-
 ?
Factor X + H2O Homo sapiens
-
 Factor Xa + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor IX + H2O
-
 Homo sapiens factor IXa + ?
-
 ?
Factor X + H2O
-
 Homo sapiens Factor Xa + ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
More structure-function relationship, overview Homo sapiens

Synonyms

Synonyms Comment Organism
FVIIa
-
 Homo sapiens
More the enzyme is a member of the trypsin family of serine proteases Homo sapiens