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Literature summary extracted from

  • Lee, C.; Lin, C.; Liu, Y.; Liu, G.; Liu, J.; Hung, H.
    Molecular interplay between the dimer interface and the substrate-binding site of human peptidylarginine deiminase 4 (2017), Sci. Rep., 7, 42662 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.3.15 expression in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.15 C434A small decrase in kcat/Km value Homo sapiens
3.5.3.15 D465A residue involved in dimerization, about 30% of wild-type catalytic effciency Homo sapiens
3.5.3.15 F285AV284A residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 F541A residue at dimer interface, about 50% decrease in kcat/Km value Homo sapiens
3.5.3.15 F576A residue at dimer interface, about 50% decrease in kcat/Km value Homo sapiens
3.5.3.15 L279A residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 L279D residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 L279I residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 L6A residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 L6D residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 L6I residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 R372A almost complete loss of activity Homo sapiens
3.5.3.15 R372K complete loss of activity Homo sapiens
3.5.3.15 R372Q almost complete loss of activity Homo sapiens
3.5.3.15 R441A residue involved in dimerization, about 6% of wild-type catalytic effciency Homo sapiens
3.5.3.15 R639A about 30% decrease in kcat/Km value Homo sapiens
3.5.3.15 V283A residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V283D residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V283I residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V283T residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V284A residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V284D residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V284I residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity Homo sapiens
3.5.3.15 V469A residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity Homo sapiens
3.5.3.15 V469L residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity Homo sapiens
3.5.3.15 V469T residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity Homo sapiens
3.5.3.15 W347A residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity Homo sapiens
3.5.3.15 W347F residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity Homo sapiens
3.5.3.15 W548A residue at dimer interface, complete loss of activity Homo sapiens
3.5.3.15 W548F residue at dimer interface, about 50% decrease in kcat/Km value Homo sapiens
3.5.3.15 W548K residue at dimer interface, about 50% decrease in kcat/Km value Homo sapiens
3.5.3.15 Y435A residue involved in dimerization, about 4% of wild-type catalytic effciency Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.15 0.1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469T, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548K, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant C434A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant D465A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F576A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279I, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.5
-
N-alpha-benzoyl-L-arginine ethyl ester wild-type, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6D, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6I, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283I, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284I, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.6
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F541A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R639A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F285A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283T, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284D, pH 7.5, 25°C Homo sapiens
3.5.3.15 1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469L, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548F, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284A, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R441A, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279D, pH 7.5, 25°C Homo sapiens
3.5.3.15 2.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant Y435A, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372A, pH 7.5, 25°C Homo sapiens
3.5.3.15 5.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469A, pH 7.5, 25°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.15 Homo sapiens Q9UM07 isoform Pad4
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.15 N-alpha-benzoyl-L-arginine ethyl ester + H2O
-
Homo sapiens N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
?

Subunits

EC Number Subunits Comment Organism
3.5.3.15 More the dimer interface and the substrate-binding site of PAD4, which consist of the I-loop and the S-loop, respectively, are responsible for substrate binding and dimer stabilization Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.3.15 PAD4
-
Homo sapiens
3.5.3.15 PADI4
-
Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.3.15 43
-
melting temperature, mutants L6D, L6I Homo sapiens
3.5.3.15 46
-
melting temperature, mutant D465A Homo sapiens
3.5.3.15 51
-
melting temperature, wild-type Homo sapiens
3.5.3.15 55
-
melting temperature, mutant V283T Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.3.15 0.04
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469T, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.07
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469L, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.12
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.6
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548K, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469A, pH 7.5, 25°C Homo sapiens
3.5.3.15 2.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R441A, pH 7.5, 25°C Homo sapiens
3.5.3.15 2.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant Y435A, pH 7.5, 25°C Homo sapiens
3.5.3.15 2.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284D, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant D465A, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.6
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279D, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 4.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6D, pH 7.5, 25°C Homo sapiens
3.5.3.15 5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R639A, pH 7.5, 25°C Homo sapiens
3.5.3.15 5.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279A, pH 7.5, 25°C Homo sapiens
3.5.3.15 5.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283T, pH 7.5, 25°C Homo sapiens
3.5.3.15 5.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284A, pH 7.5, 25°C Homo sapiens
3.5.3.15 6.2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548F, pH 7.5, 25°C Homo sapiens
3.5.3.15 6.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F285A, pH 7.5, 25°C Homo sapiens
3.5.3.15 7.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6A, pH 7.5, 25°C Homo sapiens
3.5.3.15 7.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F541A, pH 7.5, 25°C Homo sapiens
3.5.3.15 7.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374A, pH 7.5, 25°C Homo sapiens
3.5.3.15 8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant C434A, pH 7.5, 25°C Homo sapiens
3.5.3.15 8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283A, pH 7.5, 25°C Homo sapiens
3.5.3.15 9.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283I, pH 7.5, 25°C Homo sapiens
3.5.3.15 9.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F576A, pH 7.5, 25°C Homo sapiens
3.5.3.15 10.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6I, pH 7.5, 25°C Homo sapiens
3.5.3.15 10.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284I, pH 7.5, 25°C Homo sapiens
3.5.3.15 11.2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279I, pH 7.5, 25°C Homo sapiens
3.5.3.15 11.7
-
N-alpha-benzoyl-L-arginine ethyl ester wild-type, pH 7.5, 25°C Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.3.15 0.02
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.05
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R372Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469L, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.15
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469A, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V469T, pH 7.5, 25°C Homo sapiens
3.5.3.15 0.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant Y435A, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R441A, pH 7.5, 25°C Homo sapiens
3.5.3.15 1.9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279D, pH 7.5, 25°C Homo sapiens
3.5.3.15 2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548K, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284D, pH 7.5, 25°C Homo sapiens
3.5.3.15 3.7
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284A, pH 7.5, 25°C Homo sapiens
3.5.3.15 4.6
-
N-alpha-benzoyl-L-arginine ethyl ester mutant W548F, pH 7.5, 25°C Homo sapiens
3.5.3.15 6.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283T, pH 7.5, 25°C Homo sapiens
3.5.3.15 7.1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R639A, pH 7.5, 25°C Homo sapiens
3.5.3.15 8.6
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F285A, pH 7.5, 25°C Homo sapiens
3.5.3.15 8.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant D465A, pH 7.5, 25°C Homo sapiens
3.5.3.15 9
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6D, pH 7.5, 25°C Homo sapiens
3.5.3.15 9.3
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374Q, pH 7.5, 25°C Homo sapiens
3.5.3.15 11
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F541A, pH 7.5, 25°C Homo sapiens
3.5.3.15 11.1
-
N-alpha-benzoyl-L-arginine ethyl ester mutant R374A, pH 7.5, 25°C Homo sapiens
3.5.3.15 11.4
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283A, pH 7.5, 25°C Homo sapiens
3.5.3.15 12.2
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6A, pH 7.5, 25°C Homo sapiens
3.5.3.15 13.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279A, pH 7.5, 25°C Homo sapiens
3.5.3.15 19
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V283I, pH 7.5, 25°C Homo sapiens
3.5.3.15 20
-
N-alpha-benzoyl-L-arginine ethyl ester mutant C434A, pH 7.5, 25°C Homo sapiens
3.5.3.15 21.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L6I, pH 7.5, 25°C Homo sapiens
3.5.3.15 21.8
-
N-alpha-benzoyl-L-arginine ethyl ester mutant V284I, pH 7.5, 25°C Homo sapiens
3.5.3.15 23.4
-
N-alpha-benzoyl-L-arginine ethyl ester wild-type, pH 7.5, 25°C Homo sapiens
3.5.3.15 24.5
-
N-alpha-benzoyl-L-arginine ethyl ester mutant F576A, pH 7.5, 25°C Homo sapiens
3.5.3.15 28
-
N-alpha-benzoyl-L-arginine ethyl ester mutant L279I, pH 7.5, 25°C Homo sapiens