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Literature summary for 3.4.21.27 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
Search for more literature for 3.4.21.27

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
K170A/R171A/R173A catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A Homo sapiens
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
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
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
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
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
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
R37Q fXIa-R37Q mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
antithrombin
-
 Homo sapiens
C1-inhibitor C1-INH Homo sapiens
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P03951
-
-

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
factor XIa
-
 Homo sapiens
FXIa
-
 Homo sapiens

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
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