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Literature summary for 3.4.21.21 extracted from

  • Persson, E.; Kjalke, M.; Olsen, O.H.
    Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity (2001), Proc. Natl. Acad. Sci. USA, 98, 13583-13588.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K305V the ratio of turnover number to Km-value is 5.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
K337A the ratio of turnover number to Km-value is 4.4fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
L305V/K337A the ratio of turnover number to Km-value is 6.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
M298Q the ratio of turnover number to Km-value is 6.9fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
V158D/D296V/M298Q the ratio of turnover number to Km-value is 37.5fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
V158D/D296V/M298Q/K337A the ratio of turnover number to Km-value is 56.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
V158D/D296V/M298Q/L305V the ratio of turnover number to Km-value is 50fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens
V158D/D296V/M298Q/L305V/L337 the ratio of turnover number to Km-value is 100fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
antithrombin in presence of heparin, 20% loss of activity of wild-type enzyme after 15 min, 59% loss of activity of the K337A mutant enzyme after 15 min, 77% loss of activity of the L305V/K337A mutant enzyme after 15 min, 78% loss of activity of the V158D/D296V/M298Q mutant enzyme after 15 min, 87% loss of activity of the V158D/D296V/M298Q/K337A mutant enzyme after 15 min, 91% loss of activity of the V158D/D296V/M298Q/L305V/K337A mutant enzyme after 15 min, 53% loss of activity of the M298Q mutant enzyme after 15 min Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0019
-
Factor X pH 7.4, 37°C, mutant enzyme L305V/K337A Homo sapiens
0.002
-
Factor X pH 7.4, 37°C, mutant enzyme K337A Homo sapiens
0.0021
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V/L337 Homo sapiens
0.0023
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q Homo sapiens
0.0024
-
Factor X pH 7.4, 37°C, mutant enzyme M298Q Homo sapiens
0.0024
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/K337A Homo sapiens
0.0027
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V Homo sapiens
0.0029
-
Factor X pH 7.4, 37°C, wild-type enzyme Homo sapiens
0.0029
-
Factor X pH 7.4, 37°C, mutant enzyme K305V Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Ile-Pro-Arg-p-nitroanilide + H2O i.e. S2288 Homo sapiens D-Ile-Pro-Arg + p-nitroaniline
-
?
factor X + H2O
-
Homo sapiens activated factor X + ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
94
-
Factor X pH 7.4, 37°C, wild-type enzyme Homo sapiens
280
-
Factor X pH 7.4, 37°C, mutant enzyme K337A Homo sapiens
370
-
Factor X pH 7.4, 37°C, mutant enzyme L305V/K337A Homo sapiens
480
-
Factor X pH 7.4, 37°C, mutant enzyme K305V Homo sapiens
520
-
Factor X pH 7.4, 37°C, mutant enzyme M298Q Homo sapiens
2600
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q Homo sapiens
4200
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V Homo sapiens
4400
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/K337A Homo sapiens
6800
-
Factor X pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V/L337 Homo sapiens