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3.4.17.20: Carboxypeptidase U

This is an abbreviated version!
For detailed information about Carboxypeptidase U, go to the full flat file.

Word Map on EC 3.4.17.20

Reaction

release of C-terminal Arg and Lys from a polypeptide =

Synonyms

aCAP, activated thrombin activable fibrinolysis inhibitor, activated thrombin-activable fibrinolysis inhibitor, activated thrombin-activatable fibrinolysis inhibitor, active carboxypeptidase B, active thrombin-activatable fibrinolysis inhibitor, Arginine carboxypeptidase, Carboxypeptidase B, pro-, carboxypeptidase B2, Carboxypeptidase R, carboxypeptidase U, Carboxypeptidase-U, CPB2, CPR, CPU, Plasma carboxypeptidase B, plasma carboxypeptidase U, plasma CPB, plasma procarboxypeptidase B, plasma procarboxypeptidase B-like proenzyme, plasma procarboxypeptidase U, pro-pCPB, Procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U, proCPU, pTAFI, rTAFI, TAFI, TAFIa, TFAI, thrombin activable fibrinolysis inhibitor, thrombin activatable fibrinolysis inhibitor, Thrombin-activable fibrinolysis inhibitor, thrombin-activatable fibrinolysis inhibitor

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.20 Carboxypeptidase U

Engineering

Engineering on EC 3.4.17.20 - Carboxypeptidase U

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A505G
-
naturally occurring polymorphism
A93V
-
mutant is comparably to wild-type activated by thrombin, mutant is slightly less activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.205, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000169, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00043, Km (mM) (hippuryl-arginine, activated by plasmin): 0.00001, intrinsic stability of activated TAFI (half-life): 6.3 min
D87A
-
activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
I182R
-
site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I183E
-
site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I325I
-
a higher frequency of the most stable Ile325Ile proCPU is seen among carriers of FII G20210A mutation compared to the control group in comparison to Thr325Thr and Thr325Ile proCPU. In addition, proCPU as a risk factor for thrombosis is evaluated. In heterozygous carriers of FV Leiden or FII G20210A high levels of proCPU confers to an almost 4fold increased risk for spontaneous onset thrombosis. The more stable Ile325Ile proCPU seems to impose a higher risk for clinical manifestation of the thrombophilic condition
R302Q
S305C/T329I
-
generation of a stable activated thrombin activable fibrinolysis inhibitor variant by site-directed mutagenesis, the mutant's half-life is 11fold increased compared to the wild-type enzyme, the mutant also shows about 3fold higher fibrin clot lysis activityoverview
S90A
-
activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
S90D/S94V/S90D
-
mutant is not activated by thrombin or by thrombin in the presence of thrombomodulin, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00004, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000005, intrinsic stability of activated TAFI (half-life): 5.9 min
S94V
-
mutant is considerably more effectively activated by thrombin, mutant is also activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.328, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000232, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.0003, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000006, intrinsic stability of activated TAFI (half-life): 6.1 min
T147A
-
naturally occurring polymorphism
T325I
T325I/T329I/H333Y/H335Q
-
inactive mutant has a 70fold increased half-life and a 3fold to 5fold increased antifibrinolytic function as compared to wild-type, mutant aggregates into large, insoluble complexes that can be removed by centrifugation
moe
-
construction of enzyme-deficient mice by gene disruption, which is not lethal and does not cause a pathogenic phenotype, the mice show delayed wound healing, overview
additional information