Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Venkateswarlu, D.; Perera, L.; Darden, T.; Pedersen, L.G.
    Structure and dynamics of zymogen human blood coagulation factor X (2002), Biophys. J., 82, 1190-1206.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.6 Phospholipids interaction via Lys14 of the Gla-domain Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.6 G114R simulation of the exchange of residues, conserved residue in the EGF2 domain sulfide loop, disruptive salt bridge interaction or blockage of interaction with factors VIIIa/IXa Homo sapiens
3.4.21.6 G323S simulation of the exchange of residues, mutation disrupts a highly conserved beta-sheet structure Homo sapiens
3.4.21.6 N57T simulation of the exchange of residues, loss of interaction with Cys81 with structural implications Homo sapiens
3.4.21.6 P343S simulation of the exchange of residues, conserved residue involved in a suface beta-sheet, affects intrinsic folding Homo sapiens
3.4.21.6 R326C simulation of the exchange of residues, surface residue, involved in protein-protein interactions, interaction with Gln376 located in the S1-binding site Homo sapiens
3.4.21.6 T318M simulation of the exchange of residues, surface residue involved in a side-chain hydrogen bond with Glu341 which is lost in the mutant, leads to clinical effect Homo sapiens
3.4.21.6 V298M simulation of the exchange of residues, unfolding occurs due to space limitation Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.6 Ca2+ dependent on, required for coordination of the enzyme domains, residues Asp46, Gly47, Gln49, and Gly64 are involved in Ca2+ binding, modeling of the calcium-binding site within the serine protease domain Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.6 Homo sapiens P00742
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.6 proteolytic modification reorientation of the N-terminus of serine protease domain after proteolytic activation of factor X to factor Xa, cleavage of the activation peptide at the Arg194-Ile195 peptide bond Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.21.6 selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin scutelarin has similar specificity Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.6 prothrombin + H2O
-
 Homo sapiens thrombin + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.6 More schematic representation and modeling of the structure of the two peptide chains of factor X, amino acid sequence, enzyme possesses an activation peptide, a catalytic serine protease domain, a GF2 domain, and a EGF1 domain, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.21.6 blood coagulation factor X zymogen Homo sapiens
3.4.21.6 factor Xa mature enzyme Homo sapiens
3.4.21.6 fX
-
 Homo sapiens
3.4.21.6 FXa
-
 Homo sapiens
3.4.21.6 More the enzyme belongs to the peptidase family S1, i.e. trypsin family Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.6 vitamin K dependent on Homo sapiens