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3.5.3.15: protein-arginine deiminase

This is an abbreviated version!
For detailed information about protein-arginine deiminase, go to the full flat file.

Word Map on EC 3.5.3.15

Reaction

protein L-arginine
+
H2O
=
protein L-citrulline
 +
NH3

Synonyms

deiminase, protein (arginine), HL-60 PAD, hPADI2, hPADI4, hPADVI, PAD, PAD 1, PAD 2, PAD 3, PAD 4, PAD II, PAD IV, PAD type 2, PAD-4, PAD-H19, PAD-R11, PAD-R4, PAD1, PAD2, PAD3, PAD4, PAD6, PADI1, Padi2, PADI3, PADI4, peptidyl arginine deiminas 4, peptidyl arginine deiminase, peptidyl arginine deiminase 2, peptidyl-arginine deiminase, peptidylarginine deiminase, peptidylarginine deiminase 1, peptidylarginine deiminase 2, peptidylarginine deiminase 3, peptidylarginine deiminase 4, peptidylarginine deiminase 6, peptidylarginine deiminase isoform VI, peptidylarginine deiminase IV, peptidylarginine deiminase type 4, Peptidylarginine deiminase type alpha, peptidylarginine deiminase type I, peptidylarginine deiminase type II, peptidylarginine deiminase type III, peptidylarginine deiminase type VI, peptidylarginine deiminase-4, PPAD, protein arginine deiminase, protein arginine deiminase 2, protein arginine deiminase 3, protein arginine deiminase 4

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.15 protein-arginine deiminase

Engineering

Engineering on EC 3.5.3.15 - protein-arginine deiminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A112G
-
K0.5 for Ca2+ higher than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
A82V
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
A82V/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
C434A
small decrase in kcat/Km value
C645A
C647A
loss of activity
D123N
D125A
D166A
D169A
D177A
D273A/R544A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.35 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.5/sec, quaternary structure: dimer, Kd: 0.68 microM
D350A
no enzymic activity, catalytic residue
D369A
no enzymic activity, ligand for Ca2 coordination
D370A
D374A
D388A
81% of wild type activity, ligand for Ca4 coordination
D389A
D465A
residue involved in dimerization, about 30% of wild-type catalytic effciency
D473A
no enzymic activity, catalytic residue
D547A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 11.6/sec, quaternary structure: monomer/dimer, Kd: 6.4 microM
D547E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.72 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 8.9/sec, quaternary structure: monomer/dimer, Kd: 11.2 microM
D547N
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.86 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 4.9 microM
E281A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.45 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.1/sec, quaternary structure: dimer, Kd: 0.1 microM
E351A
33% of wild type activity, ligand for Ca2 coordination
E352A
E353A
no enzymic activity, ligand for Ca1 coordination
E354A
2000fold decrease in activity
E411A
no enzymic activity, ligand for Ca1 coordination
E412A
F221A/F222A
F285AV284A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
F541A
residue at dimer interface, about 50% decrease in kcat/Km value
F576A
residue at dimer interface, about 50% decrease in kcat/Km value
G374R
-
the PAD3 mutant does not display PAD4-like kinetics with benzoylated arginine derivatives
H471A
no enzymic activity, catalytic residue
L279A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L279D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L279I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
N373A
no enzymic activity, ligand for Ca2 coordination
N648A
37% of wild type activity, ligand for water-mediated Ca1 coordination
Q349A
no enzymic activity, ligand for Ca1 coordination
Q350A
R123K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R123Q
-
K0.5 for Ca2+ higher than that obtained with the R123K mutant, but lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R156K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R156Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R205K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R205Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R347A
R372A
almost complete loss of activity
R372K
R372Q
R373A
2000fold decrease in activity
R374K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R374Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R419K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R419Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R441A
residue involved in dimerization, about 6% of wild-type catalytic effciency
R484K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R484Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R609K
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R609Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lcomparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R639A
about 30% decrease in kcat/Km value
R639K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R639Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R8A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.47 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 9.3 microM
R8A/D547A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.4 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 10.7/sec, quaternary structure: monomer/dimer, Kd: 3.9 microM
R8E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 1.06 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 7.3/sec, quaternary structure: monomer, Kd: 45.6 microM
R8E/D547E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 2.77 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 3.3/sec, quaternary structure: monomer, Kd: 24 microM
R8H
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.47 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.3/sec, quaternary structure: dimer, Kd: 0.47 microM
R8K
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.5 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 10.8/sec, quaternary structure: monomer/dimer, Kd: 10.2 microM
R8L
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 1.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 5.3/sec, quaternary structure: monomer, Kd: 16.8 microM
R8Q
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.6 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 15.7 microM
S55G
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) higher than wild-type
S55G/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
S55G/A82V
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows reduced activity compared to the wild-type PADI4
S55G/A82V/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
V283A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283T
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V469A
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
V469L
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
V469T
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W347A
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W347F
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W348A
loss of activity
W373A
50fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
W548A
residue at dimer interface, complete loss of activity
W548F
residue at dimer interface, about 50% decrease in kcat/Km value
W548K
residue at dimer interface, about 50% decrease in kcat/Km value
Y237A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.9/sec, quaternary structure: dimer, Kd: 0.29 microM
Y237A/E281A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.38 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.2/sec, quaternary structure: dimer, Kd: 0.1 microM
Y435A
Y435N
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 2.73 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 4/sec, quaternary structure: monomer, Kd: 33.8 microM
DELTA1-385
-
IKKgamma co-immunoprecipitates truncation mutants, PAD2(1-385) and PAD2(355-672)
DELTA355-672
-
IKKgamma co-immunoprecipitates truncation mutants, PAD2(1-385) and PAD2(355-672)
Q358A
-
substitution of Gln-358 (a putative ligand for Ca2+ binding) with an Ala abolishes co-immunoprecipitation with IKKgamma
C351S
-
the mutant is catalytically inactive, exhibiting less than 0.01% wild type activity
R152A
significant reduction in activity
R154A
activity is similar to wild-type
C351A
-
inactive
-
R152A
-
significant reduction in activity
-
R154A
-
activity is similar to wild-type
-
additional information