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3.4.21.22: coagulation factor IXa

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

Word Map on EC 3.4.21.22

Reaction

Selective cleavage of Arg-/-Ile bond in factor X to form factor Xa =

Synonyms

activated Christmas factor, activated coagulation factor IX, activated factor IX, activated FIX, blood coagulation factor IXa, Christmas factor, circulating factor IXa, coagulation factor IX, coagulation factor IXa, factor IX, factor IXa, factor IXaAL, factor IXaalpha, factor IXabeta, factor IXabeta', factor IXaCH, factor IXalphabeta, factor IXaN, factor XIa, FIX, FIXa, FIXC, Gla-domainless factor IXabeta', human coagulation factor IXa, intrinsic Xase, More

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.22 coagulation factor IXa

Engineering

Engineering on EC 3.4.21.22 - coagulation factor IXa

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D47G
-
factor IXaAL, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
E186A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
E410A
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410H
-
the mutant with reduced hydrolytic activity and increased in-vitro clotting activity has 2.5fold enhanced affinity for the cofactor FVIIIa and induces 5.2fold higher thrombin generation compared to the wild type enzyme
E410L
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410N
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
FIXagamma225P
mutant enzyme
G94R
-
33% of wild-type vmax
Gla-domainless factor IXa
20000times lower kacat for factor X hydrolysis than wild-type
H185A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
K126A
K132A
K265A
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14 and CLB-fIX 13
K98A
site-directed mutagenesis,
K98T
the variant demonstrates a 2fold improvement in kcat/KM value for Pefa9 as compared to the wild type enzyme
K98T/R150A/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
N129A
N178A
N346D
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14, no binding of anti fIX monoclonal antibody CLB-fIX 13
R143A
4times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R145H
-
factor IXaCH, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
R147A
3times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R150
similar kcat for factor X hydrolysis as wild-type Gla-domainless factor IXa
R150A
the mutation reduces potential autolysis in the 148-loop during production and leads to reduced activity compared to the wild type enzyme
R150A/I213V
the variant shows increases in the catalytic efficiency for amidolytic activity when the target substrate is either Pefa9 or Pefa10 with 1.5fold and 1.2fold increases, respectively
R165A
R170A
-
the mutation slightly (0.5fold) reduces supersulfated low molecular weight heparin affinity
R188A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
R233A
-
the mutation dramatically (14fold) reduces supersulfated low molecular weight heparin affinity
R333Q
activation of factor X is not impaired
R94D
-
slight increase in vmax
rFIXa104A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa105A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa107A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa89A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa90A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa91A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa94A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
V16I/I21/V R150A
the variant results in a negligible increase in activity compared with the V16I/R150A variant
V16I/K98T/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/I213V/R150A
the mutations result in a 6fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/R150A
the mutant shows enhancements in activity leading to a 2.5fold increased kinetic efficiency compared with the wild type enzyme
V16I/K98T/Y177T/I213V
the variant reduces the kinetic efficiency to the 4fold increase that is also observed with the K98T/R150A/I213V variant
V16I/R150A
the variant shows no increase in the kcat/KM value for Pefa9 as compared to the wild type enzyme
Y450C
-
the mutant shows about 5% activity compared to the wild type enzyme
Y450F
-
the mutant shows about 25% activity compared to the wild type enzyme
Y450S
-
the mutant shows about 5% activity compared to the wild type enzyme
Y94F/A95aK/K98T/Y177F
-
mutation, higher clotting activity than wild type FIXa
Y94F/A95aK/K98T/Y177F/I213V/E219G
-
about 6fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F/I213V/E219G
-
about 17fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
additional information