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

BRENDA support

Literature summary for 3.4.21.21 extracted from

  • Persson, E.
    Macromolecular substrate affinity for free factor VIIa is independent of a buried protease domain N-terminus (2006), Biochem. Biophys. Res. Commun., 341, 28-32.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
FFR-FVIIa derivate of FVIIa with a stably buried N-terminus representing the active conformation of FVIIa, IC50: 0.019 mM Homo sapiens
V154G-FVIIa derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
Factor X 100 nM FVIIa, incubation for 20 min at room temperature 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 factor Xa
-
?

Synonyms

Synonyms Comment Organism
coagulation factor VII(a)
-
Homo sapiens
free factor VIIa
-
Homo sapiens
FVIIa
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00019
-
Factor X
-
Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.014
-
derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM Homo sapiens V154G-FVIIa
0.019
-
derivate of FVIIa with a stably buried N-terminus representing the active conformation of FVIIa, IC50: 0.019 mM Homo sapiens FFR-FVIIa