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Literature summary for 3.4.21.27 extracted from

  • Smith, S.B.; Verhamme, I.M.; Sun, M.F.; Bock, P.E.; Gailani, D.
    Characterization of novel forms of coagulation factor XIa. Independence of factor XIa subunits in factor IX activation (2008), J. Biol. Chem., 283, 6696-6705.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
stable expression of wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C362S/C482S site-directed mutagenesis Homo sapiens
additional information construction of FXI with a single catalytic active site, construction of recombinant FXI with the A4 domain replaced by the A4 domain from plasma prekallikrein, i.e. FXI/PKA4, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
D-Phe-Pro-Arg-CH2Cl irreversibly inhibits both active sites of the enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of isolated subunits with each one active site, stoichiometry of FIX and FIXalphabeta binding to FXIa, overview Homo sapiens
0.053
-
factor IX pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens
0.4
-
pyroGlu-Pro-Arg-4-nitroanilide pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor IX + H2O Homo sapiens two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX activated factor IX + ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification FXI activation proceeds through an intermediate with one activated subunit, limited digestion by incubating with FXIIa or thrombin Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
native enzyme from plasma and recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography with elution by benzamidine Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Homo sapiens
-
plasma
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type andmutant substrate, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor IX + H2O two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX Homo sapiens activated factor IX + ?
-
?
factor IX + H2O cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type and mutant substrate, overview Homo sapiens activated factor IX + ?
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O substrate S-299 Homo sapiens ?
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O substrate S-2366 Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX Homo sapiens

Synonyms

Synonyms Comment Organism
FXIa
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.268
-
pyroGlu-Pro-Arg-4-nitroanilide pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens
0.55
-
factor IX pH 7.4, 37°C, recombinant wild-type enzyme Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information
-
Homo sapiens