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3.4.21.27: coagulation factor XIa

This is an abbreviated version!
For detailed information about coagulation factor XIa, go to the full flat file.

Word Map on EC 3.4.21.27

Reaction

Selective cleavage of Arg-/-Ala and Arg-/-Val bonds in factor IX to form factor IXa =

Synonyms

activated blood-coagulation factor XI, activated coagulation factor XIa, activated factor XI, activated factor XIa, activated FXI, activated plasma thromboplastin antecedent, blood coagulation factor XIa, blood-coagulation factor XI, activated, blood-coagulation factor XIa, coagulation factor XI, coagulation factor XIa, factor XI, factor XIa, factor XIa catalytic domain, FXI, FXIa, fXIaCD, More, plasma thromboplastin antecedent, prolyl endopeptidase, protease factor XIa, PTA, recombinant human FXI370-607, rhFXI370-607

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.27 coagulation factor XIa

Engineering

Engineering on EC 3.4.21.27 - coagulation factor XIa

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C147S
-
inactive
C321S
-
the mutant shows wild type activity
C362S/C482S
C398Y
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
C482S
-
the mutant shows 1.45fold enhanced activity as compared with the wild type enzyme
C500S
inactive
E98A
-
the mutant has normal Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
E98D
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
E98V
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
FXI/G326C
-
mutant of FXI with Gly326 residue mutated to Cys326
G104R
this mutation in the PK A2 domain associated with CRM+ PK deficiency causes decreased kininogen binding
G155E
is a rare example of a mutation causing CRM+ FXI deficieny
G193A
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193D
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 1.6-36fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193E
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193K
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 35-478fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193R
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193V
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G400V
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
I151A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
K145A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K148A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K149A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
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
K170A/R171A/R173A
catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A
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
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
K192A
-
the mutant has normal Km value for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
K192E
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
K192Q
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
K192R
-
the mutant has decreased Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
M102T
-
site-directed mutagenesis,missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
M18I
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
P520L
-
site-directed mutagenesis, similar to the wild-ype enzyme
R144A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/K148A/K149A
site-directed mutagenesis of an autolysis loop residues, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
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)
R147A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
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
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
R3704A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
R378C
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
R37Q
fXIa-R37Q mutant
S225F
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
S248A
binds platelets with reduced affinity compared with wild-type
S248N
binds platelets with 5fold reduced affinity compared with wild-type, the A3 domain is probably not affected significantly, as FXI-Asn248 is secreted, activated by activated factor XII, and activates FIX similar to wild-type activated factor IX. Is associated with bleeding and defective FXI binding to platelets but does not affect the activated partial thromboplastin time assay, which does not contain platelets
S248Q
binds platelets with reduced affinity compared with wild-type
S434A/K437A/T475A/C482S
to improve crystallizability a quadrupole mutant is generated
S434A/T475A/C482S/K437A
site-directed mutagenesis, crystal structure determination with bound benzylamidine
T575M
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
W569S
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
Y133S
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
Y143A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
Y5901A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
Y5901V
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
additional information