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

BRENDA support

Literature summary extracted from

  • Larsen, K.S.; Östergaard, H.; Bjelke, J.R.; Olsen, O.H.; Rasmussen, H.B.; Christensen, L.; Kragelund, B.B.; Stennicke, H.R.
    Engineering the substrate and inhibitor specificities of human coagulation factor VIIa (2007), Biochem. J., 405, 429-438.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.21 purified complex between Trp-Tyr-Thr-Arg-cmk-FVIIa and sTF1?209, hanging drop vapour diffusion method, 10 mg/ml protein in 10 mM Tris-HCl, pH 7.5, 100 mM NaCl and 2 mM CaCl2, with 0.1 M sodium citrate, 16.5–15.5% w/v PEG 4000 and 12% v/v propan-1-ol, pH 5.6, as the precipitating agent, X-ray diffraction structure determination and analysis, modeling Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.21 T239A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
3.4.21.21 T239G site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
3.4.21.21 T239I site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
3.4.21.21 T239Y site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.21 antithrombin III complete inhibition Homo sapiens
3.4.21.21 Trp-Tyr-Thr-Arg-chloromethyl ketone
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.21 additional information
-
 additional information kinetics of wild-type and mutant enzymes with different substrates, overview Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.21 Ca2+
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.21 Homo sapiens
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.21 additional information
-
 catalytic efficiencies of wild-type and mutant enzymes with different substrates, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.21 4-methylumbelliferyl 4-guanidinobenzoate + H2O
-
 Homo sapiens ?
-
 ?
3.4.21.21 benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide + H2O chromogenic S-2765 Homo sapiens ?
-
 ?
3.4.21.21 D-Ile-Pro-Arg-4-nitroanilide + H2O chromogenic substrate S-2288 Homo sapiens D-Ile-Pro-Arg + 4-nitroaniline
-
 ?
3.4.21.21 Factor X + H2O FX cleavage site Asn-Leu-Thr-Ar-/-Ile-Val-Gly-Gly Homo sapiens Factor Xa + ?
-
 ?
3.4.21.21 additional information substrate and cleavage site specificity with 7-amino-4-carbamoylmethylcoumarin-linked tetrapeptides, specificity profiling of the recombinant enzyme, overview Homo sapiens ?
-
 ?
3.4.21.21 Trp-Ala-Thr-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
-
 Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.21 factor VIIa
-
 Homo sapiens
3.4.21.21 FVIIa
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.21 22
-
 assay at room temperature Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.21 7.4
-
 assay at Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.21.21 additional information
-
 additional information inhibition kinetics of wild-type and mutant enzymes, overview Homo sapiens