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Literature summary for 3.4.21.6 extracted from

  • Bianchini, E.P.; Louvain, V.B.; Marque, P.E.; Juliano, M.A.; Juliano, L.; Le Bonniec, B.F.
    Mapping of the catalytic groove preferences of factor Xa reveals an inadequate selectivity for its macromolecule substrates (2002), J. Biol. Chem., 277, 20527-20534.
    View publication on PubMed
Search for more literature for 3.4.21.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in BHK-21 cells Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substrate specificity for amino acid residues at positions P3, P2, P1', P2', and P3', overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prothrombin + H2O Homo sapiens
-
 thrombin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification processing of factor X to factor Xa can be performed with Russell's viper venom at pH 8.3 Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant facgtor X from BHK-21 cells Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin scutelarin has similar specificity, hydrolyzes two petide bonds in prothrombin having (Glu/Asp)-Gly-Arg-(Thr/Ile) as P3-P2-P1-P1' residues, glycine is not the best P2-residue, phenylalanine shows even higher activity at this position Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity and catalytic efficiency, catalytic groove structure, activity with peptide substrate is virtually the same in presence or absence of complexed factor Va, indicating that the factor Va does not allosterically control the catalytic groove, catalytic efficacy of prothrombinase complex originates from exosite interactions with factor Va and/or prothrombin Homo sapiens ?
-
 ?
prothrombin + H2O
-
 Homo sapiens thrombin + ?
-
 ?
prothrombin + H2O limited preference for the cleavage site, hydrolyzes two petide bonds in prothrombin having (Glu/Asp)-Gly-Arg-(Thr/Ile) as P3-P2-P1-P1' residues, glycine is not the best P2-residue, phenylalanine shows even higher activity at this position Homo sapiens thrombin + ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme is complexed in the prothrombinase complex with factor Va, Ca2+, and phospholipids Homo sapiens

Synonyms

Synonyms Comment Organism
factor Xa
-
 Homo sapiens
FXa
-
 Homo sapiens
More the enzyme belongs to the peptidase family S1, i.e. trypsin family Homo sapiens