3.4.21.9: enteropeptidase

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

Word Map on EC 3.4.21.9

Reaction

Activation of trypsinogen by selective cleavage of Lys6-/-Ile bond =

Synonyms

peptidase, entero-, enterokinase, EC 3.4.4.8, BEK, HEK, human enteropeptidase, bovine enteropeptidase, Chinese bovine enterokinase, EKL-His6, EK, recombinant enterokinase light chain, rEKL, recombinant His-tagged enterokinase light chain, rEKL/His, recombinant bovine enterokinase catalytic subunit protein, Chinese northern yellow bovine enterokinase catalytic subunit, EKL, natural enteropeptidase, EP 118-1035, native enterokinase, porcine enterokinase, enteropeptidase, enteropeptidase light chain, enterokinase light chain, bovine enterokinase light chain, sBEKLC, EP-1, HEP, BEP, PRSS7, TMPRSS15, L-HEP, L-BEP, EPL, L-HEK, EKLC

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.9 enteropeptidase

Engineering

Engineering on EC 3.4.21.9 - enteropeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K99A
-
no cleavage of trypsinogen or Gly-(Asp)4-Lys-beta-naphthylamide and reduced rate of inhibition by Val-(Asp)4-Lys-chloromethane
Y174R/K99M
-
site-directed mutagenesis, the mutant does not form the active structure
Y174R/K99Q
-
site-directed mutagenesis, the mutant does not form the active structure
Y174K/K99M
-
site-directed mutagenesis, the mutant does not form the active structure
Y174K/K99Q
-
site-directed mutagenesis, the mutantion results in a more site-specific enterokinase light chain
Y174K
-
site-directed mutagenesis,
Y174R
-
site-directed mutagenesis,
C112S
site-directed mutagenesis, replacement of the free cysteine residue with serine improves the refolding yield of the recombinant enzyme by 50%. The heat stability of this C112S variant was also significantly improved by supercharging
R96Q
the mutant shows decreased specificities for substrates containing the sequences DDDDK and DDDDR, while basic pancreatic trypsin inhibitor inhibition is increased
N6D/G21D/G22D/N141D/K209E
site-directed mutagenesis, the mutations lead to supercharging of the protein surface leading to 100fold increased protein solubility
Y174R
the mutant shows improved specificities for substrates containing the sequences DDDDK and DDDDR, while basic pancreatic trypsin inhibitor inhibition is significantly decreased
N6D/G21D/G22D/N142D/K210E/C112S
supercharged variant with increased solubility more than 100fold, used for crystallization
H24Q
the mutant shows slightly reduced activity compared to the wild type enzyme
E173A
site directed mutagenesis
F144A
site directed mutagenesis
K63E
site directed mutagenesis
K63A
site directed mutagenesis
K63R
site directed mutagenesis
T105E
site directed mutagenesis
F144S
site directed mutagenesis
E173K
site directed mutagenesis
P193E
site directed mutagenesis
T105A
site directed mutagenesis
P193A
site directed mutagenesis
E136Y
the mutant shows clearly reduced activity compared to the wild type enzyme
R213L
the mutant shows increased activity compared to the wild type enzyme
E136Y/R213L
the mutant shows about wild type activity
additional information