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Literature summary extracted from

  • Yang, L.; Sun, M.F.; Gailani, D.; Rezaie, A.R.
    Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor (2009), Biochemistry, 48, 1517-1524.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.27 cDNAs in expression vector pJVCMV are used to transfect HEK-293 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.27 K170A replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains Homo sapiens
3.4.21.27 K170A/R171A/R173A catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A Homo sapiens
3.4.21.27 K175A replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains Homo sapiens
3.4.21.27 K179A replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains Homo sapiens
3.4.21.27 additional information mutations in the fXIa 170 helix are introduced into a modified human fXI cDNA (fXI-Ser-362,482), which contains serine substitutions for Cys-362 and Cys-482 Homo sapiens
3.4.21.27 R144A/K145A/R147A/R149A contains Ala substitutions for Arg-144, Lys-145, Arg-147, and Arg-149 (residues 504, 505, 507, and 509, respectively, in fXI numbering) Homo sapiens
3.4.21.27 R171A replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains Homo sapiens
3.4.21.27 R173A replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains Homo sapiens
3.4.21.27 R37Q fXIa-R37Q mutant Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.27 antithrombin
-
 Homo sapiens
3.4.21.27 C1-inhibitor C1-INH Homo sapiens
3.4.21.27 additional information heparin accelerates inhibition of factor XIa. Heparin enhances antithrombin inhibition of catalytic domain-wild-type 212fold, but only 37-94fold for catalytic domain mutants Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.27 0.552
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K170A/R171A/R173A mutant Homo sapiens
3.4.21.27 0.655
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K170A mutant Homo sapiens
3.4.21.27 0.757
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-wild type Homo sapiens
3.4.21.27 0.764
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K179A mutant Homo sapiens
3.4.21.27 0.81
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-R173A mutant Homo sapiens
3.4.21.27 0.812
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-R171A mutant Homo sapiens
3.4.21.27 0.829
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K175A mutant Homo sapiens
3.4.21.27 0.943
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-wild type Homo sapiens
3.4.21.27 0.993
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-R37Q mutant Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.27 362500
-
 catalytic domain, wild-type, SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.27 Homo sapiens P03951
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.27 affinity chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.27 plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.27 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
-
 Homo sapiens L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.27 factor XIa
-
 Homo sapiens
3.4.21.27 FXIa
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.27 98
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K170A mutant Homo sapiens
3.4.21.27 115
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K170A/R171A/R173A mutant Homo sapiens
3.4.21.27 115
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-R171A mutant Homo sapiens
3.4.21.27 116
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K179A mutant Homo sapiens
3.4.21.27 117
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-K175A mutant Homo sapiens
3.4.21.27 117
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-R173A mutant Homo sapiens
3.4.21.27 119
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-catalytic domain-wild type Homo sapiens
3.4.21.27 148
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-R37Q mutant Homo sapiens
3.4.21.27 148
-
 L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide fXIa-wild type Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.27 additional information fondaparinux pentasaccharide, all catalytic domains exhibit similar inhibition to catalytic domain-wild-type by antithrombin in the absence and presence of fondaparinux Homo sapiens