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Literature summary for 3.4.21.21 extracted from

  • Persson, E.; Nielsen, L.S.; Olsen, O.H.
    Substitution of aspartic acid for methionine-306 in factor VIIa abolishes the allosteric linkage between the active site and the binding interface with tissue factor (2001), Biochemistry, 40, 3251-3256.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in BHK cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
M306D mutation abolishes the allosteric linkage between the active site and the binding interface with tissue factor. 2fold increase in amidolytic activity. In sharp contrast to the wild-type enzyme its binding kinetic to soluble tissue factor are unaltered after inactivation with D-Phe-Phe-Arg chloromethyl ketone Homo sapiens
M306N amidolytic activity of the mutant enzyme is stimulated 7fold Homo sapiens
M306N/N309S amidolytic activity of the mutant enzyme is stimulated 1.5fold Homo sapiens
M306S amidolytic activity of the mutant enzyme is stimulated 9fold Homo sapiens
M306T amidolytic activity of the mutant enzyme is stimulated 12fold Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00071
-
Factor X mutant enzyme M306D Homo sapiens
0.00105
-
Factor X wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor X + H2O
-
Homo sapiens activated factor X + ?
-
?