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Information on EC 3.5.3.15 - protein-arginine deiminase
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3.5.3.15 protein-arginine deiminaseIUBMB Comments
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
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Word Map
- 3.5.3.15
-
citrullination
-
rheumatoid
- arthritis
- histone
- autoimmune
-
deimination
- autoantibody
-
anti-citrullinated
- chromatin
-
acpas
- epitope
- synovial
-
padis
- porphyromonas
-
anti-ccp
-
netosis
- periodontitis
- gingivalis
- sclerosis
- fibrinogen
-
anti-cyclic
- vimentin
-
hla-drb1
- elastase
- autoantigens
- ptpn22
-
decondensation
- cl-amidine
-
lupus
- erythematosus
- myeloperoxidase
- pharmacology
-
self-antigens
-
ra-associated
-
gingipains
- synoviocytes
-
rheumatology
- medicine
-
arginyl
-
erosive
- analysis
- drug development
- fibrin
-
non-hla
- filaggrin
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
padi4, peptidylarginine deiminase, padi2, peptidyl arginine deiminase, peptidylarginine deiminase 4, padi3, pad-4, padi1, protein arginine deiminase, peptidylarginine deiminase type 4, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deiminase, protein (arginine)
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-
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HL-60 PAD
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-
-
-
PAD
PAD-H19
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-
-
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PAD-R11
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-
-
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PAD-R4
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-
-
-
PAD1
PAD2
PAD3
PAD4
PAD6
PADI4
peptidyl arginine deiminase
peptidylarginine deiminase
peptidylarginine deiminase 2
peptidylarginine deiminase 4
peptidylarginine deiminase IV
Peptidylarginine deiminase type alpha
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-
-
-
PPAD
protein arginine deiminase
protein arginine deiminase 4
PAD
-
-
-
-
PAD4
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peptidylarginine deiminase
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-
-
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peptidylarginine deiminase
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protein arginine deiminase
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-
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein L-arginine + H2O = protein L-citrulline + NH3
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
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-
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
protein-L-arginine iminohydrolase
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
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CAS REGISTRY NUMBER
COMMENTARY
75536-80-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-[3-(2,5-dioxo-1-phenylimidazolidin-4-yl)propyl]guanidine + H2O
N-[3-(2,5-dioxo-1-phenylimidazolidin-4-yl)propyl]urea + NH3
-
-
-
?
1-[3-(2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepin-3-yl)propyl]guanidine + H2O
N-[[6-(benzyloxy)-1H-indol-2-yl]methyl]urea + NH3
-
-
-
?
1-[3-(2,5-dioxoimidazolidin-4-yl)propyl]guanidine + H2O
N-[3-(2,5-dioxoimidazolidin-4-yl)propyl]urea + NH3
-
-
-
?
1-[3-[1-(biphenyl-3-ylmethyl)-2,5-dioxoimidazolidin-4-yl]propyl]guanidine + H2O
N-(3-[1-[([1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)urea + NH3
-
-
-
?
1-[[6-(benzyloxy)-1H-indol-2-yl]methyl]guanidine + H2O
N-[[6-(benzyloxy)-1H-indol-2-yl]methyl]urea + NH3
-
-
-
?
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + H2O
2-acetyl-Gly-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + NH3
-
-
-
-
?
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + H2O
3-acetyl-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + NH3
-
-
-
-
?
4-carbamimidamido-N-(diphenylmethyl)butanamide + H2O
4-(carbamoylamino)-N-(diphenylmethyl)butanamide + NH3
-
-
-
?
4-[4-(3-carbamimidamidopropyl)-2,5-dioxoimidazolidin-1-yl]-2-ethoxy-N-(4-methoxyphenyl)benzamide + H2O
4-[4-[3-(carbamoylamino)propyl]-2,5-dioxoimidazolidin-1-yl]-2-ethoxy-N-(4-methoxyphenyl)benzamide + NH3
-
-
-
?
4-[4-(3-carbamimidamidopropyl)-2,5-dioxoimidazolidin-1-yl]-N-(4-methoxyphenyl)benzamide + H2O
4-[4-[3-(carbamoylamino)propyl]-2,5-dioxoimidazolidin-1-yl]-N-(4-methoxyphenyl)benzamide + NH3
-
-
-
?
4-[4-(3-carbamimidamidopropyl)-2,5-dioxoimidazolidin-1-yl]-N-phenylbenzamide + H2O
4-[4-[3-(carbamoylamino)propyl]-2,5-dioxoimidazolidin-1-yl]-N-phenylbenzamide + NH3
-
-
-
?
4-[4-[3-(carbamoylamino)propyl]-2,5-dioxoimidazolidin-1-yl]-N-(4-methoxyphenyl)benzamide + H2O
4-[4-[3-(carbamoylamino)propyl]-2,5-dioxoimidazolidin-1-yl]-2-methoxy-N-(4-methoxyphenyl)benzamide + NH3
-
-
-
?
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys-Arg-His-Arg-acetyl-Lys-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly + H2O
Ac-Ser-Gly-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly + NH3
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala + H2O
Ac-Ser-Gly-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala + NH3
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + H2O
Ac-Ser-Gly-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys + NH3
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val + H2O
?
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val + H2O
Ac-Ser-Gly-Cit-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val + NH3
-
-
-
-
?
benzoyl-Arg methyl ester + H2O
benzoyl-citrulline methyl ester + NH3
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-
-
-
?
benzoyl-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-citrulline-4-methylcoumarin-7-amide + NH3
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-
-
-
?
benzoyl-D-Arg-p-nitroanilide + H2O
benzoyl-citrulline-p-nitroanilide + NH3
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18% of the rate of the L-isomer
-
-
?
benzoyl-homoarginine ethyl ester + H2O
(2S)-2-aminobenzoyl-6-[(aminocarbonyl)amino]hexanoic acid + NH3
-
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-citrulline-p-nitroanilide + NH3
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-
-
-
?
benzoyl-L-arginine methyl ester + H2O
benzoyl-L-citrulline methyl ester + NH3
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-citrulline-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
beta-actin L-arginine + H2O
beta-actin L-citrulline + NH3
substrate for isoform PAD2 only
-
-
?
citrullinated histone H3 L-arginine + H2O
?
substrate for isoform PAD4 only
-
-
?
CRGKA + H2O
?
-
Giardia lamblia ADI specifically binds to and citrullinates the arginine in the conserved CRGKA tail of variant-specific surface proteins affecting both antigenic switching and antibody mediated cell death
-
-
?
CXCL5-L-Arg + H2O
CXCL5-L-citrulline + NH3
-
PAD site-specifically deiminates L-Arg9 in CXCL5 to L-citrulline
-
-
?
filaggrin L-Arg + H2O
filaggrin citrulline + NH3
-
-
-
?
gamma-actin L-arginine + H2O
gamma-actin L-citrulline + NH3
substrate for isoform PAD2 only
-
-
?
glial fibrillary acidic protein L-arginine + H2O
glial fibrillary acidic protein L-citrulline + NH3
-
-
-
?
glial fibrillary acidic protein-L-Arg + H2O
glial fibrillary acidic protein-L-citrulline + NH3
-
-
-
?
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
glycogen phosphorylase b + H2O
?
-
specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP
-
-
?
glycogen phosphorylase b + H2O
? + NH3
-
specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP
-
-
?
heat shock protein 8 L-Arg + H2O
heat shock protein 8 L-citrulline + NH3
-
-
-
?
histone H2A L-arginine + H2O
histone H2A L-citrulline + NH3
-
deimination occurs at Arg3 of the N-terminal sequence acetyl-SGRGK
-
-
?
histone H3 L-Arg + H2O
histone H3 L-citrulline + NH3
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citrullination activity is limited to diestrus with histone H3
-
-
?
histone H4 L-arginine + H2O
histone H4 L-citrulline + NH3
-
deimination occurs at Arg3 of the N-terminal sequence acetyl-SGRGK
-
-
?
human vimentin L-arginine + H2O
human vimentin L-citrulline + NH3
-
-
-
-
?
L-Arg-Gly + H2O
L-Cit-Gly + NH3
-
75% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-Arg-Gly-Gly + H2O
L-Cit-Gly-Gly + NH3
-
66% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-canavanine + H2O
? + NH3
-
0.3% activity compared to L-arginine
-
-
?
L-homoarginine + H2O
? + NH3
-
0.3% activity compared to L-arginine
-
-
?
L-Leu-Trp-Met-Arg + H2O
L-Leu-Trp-Met-Cit + NH3
-
45% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-Met-Arg-Phe + H2O
L-Met-Cit-Phe + NH3
-
the substrate shows fastest rate of citrullination with 158% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-octopine + H2O
? + NH3
-
16.7% activity compared to L-arginine
-
-
?
myelin basic protein-L-Arg + H2O
myelin basic protein-L-citrulline + NH3
-
-
-
?
N-(3-[1-[(2'-chloro-3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)guanidine + H2O
N-(3-[1-[(2'-chloro-3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)urea + NH3
-
-
-
?
N-(3-[1-[(2'-chloro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)guanidine + H2O
N-(3-[1-[(2'-chloro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)urea + NH3
-
-
-
?
N-(3-[1-[([1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)urea + H2O
N-(3-[1-[(3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl]propyl)urea + NH3
-
-
-
?
N-(biphenyl-3-ylmethyl)-4-carbamimidamidobutanamide + H2O
N-[([1,1''-biphenyl]-3-yl)methyl]-4-(carbamoylamino)butanamide + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine amide + H2O
N-alpha-benzoyl-L-citrulline amide + NH3
-
best small molecule substrate for isozyme PAD1
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline methyl ester + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine methyl ester + H2O
N-alpha-benzoyl-L-citrulline methyl ester + NH3
-
-
-
-
?
N-[(1R)-1-(biphenyl-3-yl)ethyl]-4-carbamimidamidobutanamide + H2O
N-[(1R)-1-([1,1''-biphenyl]-3-yl)ethyl]-4-(carbamoylamino)butanamide + NH3
-
-
-
?
N-[(1S)-1-(biphenyl-3-yl)ethyl]-4-carbamimidamidobutanamide + H2O
N-[(1S)-1-([1,1''-biphenyl]-3-yl)ethyl]-4-(carbamoylamino)butanamide + NH3
-
-
-
?
N-[(3'-bromobiphenyl-3-yl)methyl]-4-carbamimidamidobutanamide + H2O
N-[(3''-bromo[1,1''-biphenyl]-3-yl)methyl]-4-(carbamoylamino)butanamide + NH3
-
-
-
?
Nalpha-benzoyl L-arginine ethyl ester + H2O
Nalpha-benzoyl L-citrulline ethyl ester + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine methyl ester + H2O
Nalpha-benzoyl-L-citrulline methyl ester + NH3
neuron-specific enolase 2 L-Arg + H2O
neuron-specific enolase 2 L-citrulline + NH3
-
-
-
?
neuron-specific-enolase1 + H2O
[neuron-specific]-enolase1 L-citrulline + NH3
-
-
-
-
?
PAD4-L-arginine + H2O
PAD4-L-citrulline + NH3
-
PAD4 is autodeiminated in a time-dependent manner
-
-
?
peptide H3-1-L-arginine + H2O
peptide H3-1-L-citrulline + NH3
i.e. Ac4KQTARKSTGG13
-
-
?
peptide H3-2-L-arginine + H2O
peptide H3-2-L-citrulline + NH3
i.e. Ac14KAPRKQLATK23
-
-
?
peptide H4-L-arginine + H2O
peptide H4-L-citrulline + NH3
-
i.e. Ac1SGRGKGGKGL10
-
?
peptidylprolyl isomerase A L-Arg + H2O
peptidylprolyl isomerase A L-citrulline + NH3
-
-
-
?
protamine + H2O
? + NH3
-
peptidyl arginine deiminase III shows highest activity towards
-
-
?
S100A3-L-arginine + H2O
S100A3-L-citrulline + NH3
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide + H2O
? + NH3
-
-
-
-
?
t-butyloxycarbonyl-Leu-Gly-Arg-4-methylcoumarin-7-amide + H2O
t-butyloxycarbonyl-Leu-Gly-citrulline-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methylcoumarin-7-amide + H2O
t-butyloxycarbonyl-Leu-Lys-citrulline-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
t-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumarin-7-amide + H2O
t-butyloxycarbonyl-Leu-Thr-citrulline-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
t-butyloxycarbonyl-Val-Pro-citrulline-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
variant-specific surface protein L-arginine + H2O
variant-specific surface protein L-citrulline + NH3
-
-
-
-
?
voltage-dependent anion channel 1 L-Arg + H2O
voltage-dependent anion channel 1 L-citrulline + NH3
-
-
-
?
yeast enolase L-arginine + H2O
yeast enolase L-citrulline + NH3
-
-
-
-
?
[mitochondrial malate dehydrogenase 2]-L-arginine + H2O
[mitochondrial malate dehydrogenase 2]-L-citrulline + NH3
-
-
-
?
acetyl-L-Arg + H2O
acetyl-L-citrulline + NH3
peptidylarginine deiminase 1
-
-
?
acetyl-L-Arg methyl ester + H2O
acetyl-L-citrulline methyl ester + NH3
peptidylarginine deiminase 1
-
-
?
acetyl-L-Arg methyl ester + H2O
acetyl-L-citrulline methyl ester + NH3
peptidylarginine deiminase 2
-
-
?
acetyl-L-Arg methyl ester + H2O
acetyl-L-citrulline methyl ester + NH3
peptidylarginine deiminase 3
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
peptidyl arginine deiminase II shows highest activity towards
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + NH3
-
-
-
-
?
benzoyl-Arg-ethyl ester + H2O
benzoyl-citrulline-ethyl ester + NH3
-
hPADI2
-
-
?
benzoyl-Arg-ethyl ester + H2O
benzoyl-citrulline-ethyl ester + NH3
-
hPADI4
-
-
?
benzoyl-Arg-methyl ester + H2O
benzoyl-citrulline-methyl ester + NH3
-
hPADI2
-
-
?
benzoyl-Arg-methyl ester + H2O
benzoyl-citrulline-methyl ester + NH3
-
hPADI4
-
-
?
benzoyl-L-Arg + H2O
benzoyl-L-citrulline + NH3
peptidylarginine deiminase 1
-
-
?
benzoyl-L-Arg + H2O
benzoyl-L-citrulline + NH3
peptidylarginine deiminase 2
-
-
?
benzoyl-L-Arg + H2O
benzoyl-L-citrulline + NH3
peptidylarginine deiminase 3
-
-
?
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
peptidylarginine deiminase 1
-
-
?
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
peptidylarginine deiminase 2
-
-
?
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
peptidylarginine deiminase 3
-
-
?
benzoyl-L-Arg-NH2 + H2O
benzoyl-L-citrullineamide + NH3
-
peptidyl arginine deiminase I shows highest activity towards
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin + H2O
? + NH3
-
-
-
-
?
CESSSHHPGIAEFPS-R + H2O
CESSSHHPGIAEFPS-citrulline + NH3
i.e. fibrinogen peptide FibA-R
-
-
?
CESSSHHPGIAEFPS-R + H2O
CESSSHHPGIAEFPS-citrulline + NH3
i.e. fibrinogen peptide FibA-R
-
-
?
CXC chemokine ligand 10 L-Arg + H2O
CXC chemokine ligand 10 citrulline + NH3
-
-
-
-
?
CXC chemokine ligand 10 L-Arg + H2O
CXC chemokine ligand 10 citrulline + NH3
-
-
-
-
?
CXC chemokine ligand 11 L-arginine + H2O
CXC chemokine ligand 11 L-citrulline + NH3
-
-
-
-
?
CXC chemokine ligand 11 L-arginine + H2O
CXC chemokine ligand 11 L-citrulline + NH3
-
-
-
-
?
CXCL8 L-Arg + H2O
CXCL8 L-citrulline + NH3
citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
-
-
?
CXCL8 L-Arg + H2O
CXCL8 L-citrulline + NH3
-
citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
-
-
?
DSHKFDRDFIYSD + H2O
DSHKFDCitDFIYSD + NH3
79% conversion by isoform PAD4
-
-
?
DSHKFDRDFIYSD + H2O
DSHKFDCitDFIYSD + NH3
90% conversion by isoform PAD2
-
-
?
DSHKHSREWLWSD + H2O
DSHKHSCitEWLWSD + NH3
51% conversion by isoform PAD4
-
-
?
DSHKHSREWLWSD + H2O
DSHKHSCitEWLWSD + NH3
97% conversion by isoform PAD2
-
-
?
DSHKWHRDFFYSD + H2O
DSHKWHCitDFFYSD + NH3
73% conversion by isoform PAD4
-
-
?
DSHKWHRDFFYSD + H2O
DSHKWHCitDFFYSD + NH3
92% conversion by isoform PAD2
-
-
?
DSKFAFRGGIASD + H2O
DSKFAFCitGGIASD + NH3
25% conversion by isoform PAD4
-
-
?
DSKFAFRGGIASD + H2O
DSKFAFCitGGIASD + NH3
90% conversion by isoform PAD2
-
-
?
DSKFHFRYAVASD + H2O
DSKFHFCitYAVASD + NH3
92% conversion by isoform PAD2
-
-
?
DSKFHFRYAVASD + H2O
DSKFHFCitYAVASD + NH3
less than 20% conversion by isoform PAD4
-
-
?
DSKFKFRYAYASD + H2O
DSKFKFCitYAYASD + NH3
91% conversion by isoform PAD2
-
-
?
DSKFKFRYAYASD + H2O
DSKFKFCitYAYASD + NH3
less than 20% conversion by isoform PAD4
-
-
?
DSKHFHRDFIYSD + H2O
DSKHFHCitDFIYSD + NH3
69% conversion by isoform PAD4
-
-
?
DSKHFHRDFIYSD + H2O
DSKHFHCitDFIYSD + NH3
94% conversion by isoform PAD2
-
-
?
DSKHKSRDFVYSD + H2O
DSKHKSCitDFVYSD + NH3
69% conversion by isoform PAD4
-
-
?
DSKHKSRDFVYSD + H2O
DSKHKSCitDFVYSD + NH3
94% conversion by isoform PAD2
-
-
?
DSKHLSREWMWSD + H2O
DSKHLSCitEWMWSD + NH3
54% conversion by isoform PAD4
-
-
?
DSKHLSREWMWSD + H2O
DSKHLSCitEWMWSD + NH3
95% conversion by isoform PAD2
-
-
?
DSKKFDRDHLYSD + H2O
DSKKFDCitDHLYSD + NH3
77% conversion by isoform PAD4
-
-
?
DSKKFDRDHLYSD + H2O
DSKKFDCitDHLYSD + NH3
90% conversion by isoform PAD2
-
-
?
DSKKFDRGHLYSD + H2O
DSKKFDCitGHLYSD + NH3
80% conversion by isoform PAD4
-
-
?
DSKKFDRGHLYSD + H2O
DSKKFDCitGHLYSD + NH3
90% conversion by isoform PAD2
-
-
?
DSKKFHRDFLYSD + H2O
DSKKFHCitDFLYSD + NH3
64% conversion by isoform PAD4
-
-
?
DSKKFHRDFLYSD + H2O
DSKKFHCitDFLYSD + NH3
97% conversion by isoform PAD2
-
-
?
DSKKFHRGFLYSD + H2O
DSKKFHCitGFLYSD + NH3
100% conversion by isoform PAD2
-
-
?
DSKKFHRGFLYSD + H2O
DSKKFHCitGFLYSD + NH3
73% conversion by isoform PAD4
-
-
?
DSKKFKRDFLFSD + H2O
DSKKFKCitDFLFSD + NH3
35% conversion by isoform PAD4
-
-
?
DSKKFKRDFLFSD + H2O
DSKKFKCitDFLFSD + NH3
97% conversion by isoform PAD2
-
-
?
DSKKHDRDHLWSD + H2O
DSKKHDCitDHLWSD + NH3
80% conversion by isoform PAD4
-
-
?
DSKKHDRDHLWSD + H2O
DSKKHDCitDHLWSD + NH3
95% conversion by isoform PAD2
-
-
?
DSKKHFRDKLYSD + H2O
DSKKHFCitDKLYSD + NH3
37% conversion by isoform PAD4
-
-
?
DSKKHFRDKLYSD + H2O
DSKKHFCitDKLYSD + NH3
92% conversion by isoform PAD2
-
-
?
DSKKHFRGKLYSD + H2O
DSKKHFCitGKLYSD + NH3
22% conversion by isoform PAD4
-
-
?
DSKKHFRGKLYSD + H2O
DSKKHFCitGKLYSD + NH3
96% conversion by isoform PAD2
-
-
?
DSKKKHREWVWSD + H2O
DSKKKHCitEWVWSD + NH3
100% conversion by isoform PAD2
-
-
?
DSKKKHREWVWSD + H2O
DSKKKHCitEWVWSD + NH3
72% conversion by isoform PAD4
-
-
?
DSKKLHRDHMESD + H2O
DSKKLHCitDHMESD + NH3
65% conversion by isoform PAD4
-
-
?
DSKKLHRDHMESD + H2O
DSKKLHCitDHMESD + NH3
90% conversion by isoform PAD2
-
-
?
DSKKYDRDFLWSD + H2O
DSKKYDCitDFLWSD + NH3
76% conversion by isoform PAD4
-
-
?
DSKKYDRDFLWSD + H2O
DSKKYDCitDFLWSD + NH3
92% conversion by isoform PAD2
-
-
?
DSKKYDRGFLWSD + H2O
DSKKYDCitGFLWSD + NH3
81% conversion by isoform PAD4
-
-
?
DSKKYDRGFLWSD + H2O
DSKKYDCitGFLWSD + NH3
93% conversion by isoform PAD2
-
-
?
DSKWHHRDHLYSD + H2O
DSKWHHCitDHLYSD + NH3
71% conversion by isoform PAD4
-
-
?
DSKWHHRDHLYSD + H2O
DSKWHHCitDHLYSD + NH3
90% conversion by isoform PAD2
-
-
?
DSKWHHRGHLYSD + H2O
DSKWHHCitGHLYSD + NH3
71% conversion by isoform PAD4
-
-
?
DSKWHHRGHLYSD + H2O
DSKWHHCitGHLYSD + NH3
96% conversion by isoform PAD2
-
-
?
DSKWYHRNKFWSD + H2O
DSKWYHCitNKFWSD + NH3
45% conversion by isoform PAD4
-
-
?
DSKWYHRNKFWSD + H2O
DSKWYHCitNKFWSD + NH3
98% conversion by isoform PAD2
-
-
?
DSQFAFRGASASD + H2O
DSQFAFCitGASASD + NH3
less than 20% conversion by isoform PAD2
-
-
?
DSQFAFRGASASD + H2O
DSQFAFCitGASASD + NH3
less than 20% conversion by isoform PAD4
-
-
?
DSQWAFRHALFSD + H2O
DSQWAFCitHALFSD + NH3
95% conversion by isoform PAD2
-
-
?
DSQWAFRHALFSD + H2O
DSQWAFCitHALFSD + NH3
less than 20% conversion by isoform PAD4
-
-
?
FFDSHKFDRDFIYSD + H2O
FFDSHKFDCitDFIYSD + NH3
94% conversion by isoform PAD4
-
-
?
FFDSHKFDRDFIYSD + H2O
FFDSHKFDCitDFIYSD + NH3
97% conversion by isoform PAD2
-
-
?
FFDSHKHSREWLWSD + H2O
FFDSHKHSCitEWLWSD + NH3
22% conversion by isoform PAD4
-
-
?
FFDSHKHSREWLWSD + H2O
FFDSHKHSCitEWLWSD + NH3
96% conversion by isoform PAD2
-
-
?
FFDSHKKSREYVFSD + H2O
FFDSHKKSCitEYVFSD + NH3
100% conversion by isoform PAD2
-
-
?
FFDSHKKSREYVFSD + H2O
FFDSHKKSCitEYVFSD + NH3
58% conversion by isoform PAD4
-
-
?
FFDSHKLHREWMWSD + H2O
FFDSHKLHCitEWMWSD + NH3
91% conversion by isoform PAD4
-
-
?
FFDSHKLHREWMWSD + H2O
FFDSHKLHCitEWMWSD + NH3
92% conversion by isoform PAD2
-
-
?
FFDSHKWHRDFFYSD + H2O
FFDSHKWHCitDFFYSD + NH3
88% conversion by isoform PAD4
-
-
?
FFDSHKWHRDFFYSD + H2O
FFDSHKWHCitDFFYSD + NH3
9% conversion by isoform PAD2
-
-
?
FFDSKHFDREWIWSD + H2O
FFDSKHFDCitEWIWSD + NH3
89% conversion by isoform PAD4
-
-
?
FFDSKHFDREWIWSD + H2O
FFDSKHFDCitEWIWSD + NH3
94% conversion by isoform PAD2
-
-
?
FFDSKHKSRDFVYSD + H2O
FFDSKHKSCitDFVYSD + NH3
77% conversion by isoform PAD4
-
-
?
FFDSKHKSRDFVYSD + H2O
FFDSKHKSCitDFVYSD + NH3
92% conversion by isoform PAD2
-
-
?
FFDSKHLSREWMWSD + H2O
FFDSKHLSCitEWMWSD + NH3
73% conversion by isoform PAD4
-
-
?
FFDSKHLSREWMWSD + H2O
FFDSKHLSCitEWMWSD + NH3
97% conversion by isoform PAD2
-
-
?
FFDSKKFSRDHIESD + H2O
FFDSKKFSCitDHIESD + NH3
63% conversion by isoform PAD4
-
-
?
FFDSKKFSRDHIESD + H2O
FFDSKKFSCitDHIESD + NH3
90% conversion by isoform PAD2
-
-
?
FFDSKKKHREWVWSD + H2O
FFDSKKKHCitEWVWSD + NH3
76% conversion by isoform PAD4
-
-
?
FFDSKKKHREWVWSD + H2O
FFDSKKKHCitEWVWSD + NH3
99% conversion by isoform PAD2
-
-
?
FFDSKKWSREYFFSD + H2O
FFDSKKWSCitEYFFSD + NH3
76% conversion by isoform PAD4
-
-
?
FFDSKKWSREYFFSD + H2O
FFDSKKWSCitEYFFSD + NH3
94% conversion by isoform PAD2
-
-
?
fibrin L-arginine + H2O
fibrin L-citrulline + NH3
-
citrullinated fibrin is a potential antigen of rheumatoid arthritis
-
-
?
fibrinogen-L-arginine + H2O
fibrinogen-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
fibrinogen-L-arginine + H2O
fibrinogen-L-citrulline + NH3
PAD4
-
-
ir
filaggrin + H2O
? + NH3
-
deimination of protein-bound Arg residues to citrulline, the substrate has little structural order, the reaction proceeds rapidly to about 95% completion und results in loss of the organized structure
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
isoform PAD1
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
isoform PAD3
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
peptidylarginine deiminase 1
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
peptidylarginine deiminase 2
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
peptidylarginine deiminase 3
-
-
?
filaggrin-L-arginine + H2O
filaggrin-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
filaggrin-L-arginine + H2O
filaggrin-L-citrulline + NH3
PAD4
-
-
ir
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
PAD2, involvement in Alzheimer's diease
-
-
ir
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
PAD2
-
-
ir
Gly-Gly-L-Arg + H2O
Gly-Gly-L-Cit + NH3
-
88% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Gly-Gly-L-Arg + H2O
Gly-Gly-L-Cit + NH3
-
88% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Gly-L-Arg + H2O
Gly-L-Cit + NH3
-
130% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Gly-L-Arg + H2O
Gly-L-Cit + NH3
-
130% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
histone H2A-L-arginine + H2O
histone H2A-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone H2A-L-arginine + H2O
histone H2A-L-citrulline + NH3
PAD4
-
-
ir
histone H3-L-Arg + H2O
histone H3-L-citrulline
-
PADI4 is a histone H3-specific arginine deiminase. Deimination is a mechanism for antagonizing the transcriptional induction mediated by arginine methylation
-
-
?
histone H3-L-Arg + H2O
histone H3-L-citrulline
-
PADI4 is a histone H3-specific arginine deiminase
-
-
?
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
PAD4
-
-
ir
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
PAD4 interacts with p53 and is recruited to the p21 promoter to regulate histone H3 L-Arg methylation and citrullination
-
-
?
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
PAD4
-
-
ir
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
-
isozyme PAD4 deiminates histone H4 at arginines 3, 17, and 19 in vitro and arginine 3 in vivo
-
-
?
histone L-arginine + H2O
histone L-citrulline + NH3
-
PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones
-
-
?
IHAREIFDSR + H2O
IHAREIFDS-citrulline + NH3
peptide derived from enolase
-
-
?
IHAREIFDSR + H2O
IHAREIFDS-citrulline + NH3
-
peptide derived from enolase
-
-
?
IHAREIFDSR + H2O
IHAREIFDS-citrulline + NH3
peptide derived from enolase
-
-
?
keratin + H2O
? + NH3
-
peptidylarginine deiminase type I acts on the arginine residue in the V2 subdomain of mouse keratin more readily than peptidylarginine deiminase type II
-
-
?
keratin L-arginine + H2O
keratin L-citrulline + NH3
peptidylarginine deiminase 1
-
-
?
keratin L-arginine + H2O
keratin L-citrulline + NH3
peptidylarginine deiminase 2
-
-
?
keratin L-arginine + H2O
keratin L-citrulline + NH3
peptidylarginine deiminase 3
-
-
?
keratin-L-arginine + H2O
keratin-L-citrulline + NH3
PAD2, involvement in psoriasis
-
-
ir
keratin-L-arginine + H2O
keratin-L-citrulline + NH3
PAD2
-
-
ir
L-arginine + H2O
L-citrulline + NH3
-
28% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
28% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-arginine-methyl ester + H2O
L-citrulline methyl ester + NH3
isoform PAD1 shows 15% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
L-arginine-methyl ester + H2O
L-citrulline methyl ester + NH3
isoform PAD3 shows 15% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
myelin basic protein + H2O
?
-
decreased methylation of myelin basic protein possibly by a shortage of S-adenosylmethionine or downregulation of the methyltransferase gen expression allows the peptidylarginine deiminase greater access to the arginyl groups of myelin basic protein
-
-
?
myelin basic protein L-arginine + H2O
myelin basic protein L-citrulline + NH3
-
-
-
-
?
myelin basic protein L-arginine + H2O
myelin basic protein L-citrulline + NH3
-
-
-
?
myelin basic protein L-arginine + H2O
myelin basic protein L-citrulline + NH3
PAD2 overexpression in brain of transgenic mice leads to myelin loss in the central nervous system
-
-
?
myelin basic protein L-arginine + H2O
myelin basic protein L-citrulline + NH3
-
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
PAD2 and PAD4 are involved in the pathogenesis of demyelination diseases such as multiple sclerosis, overview
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
PAD2, involvement in multiple sclerosis
-
-
ir
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
amino acid sequence determination of the substrate protein by LC/MS, PAD2 deiminates 18 of 19 arginyl residues, whereas PAD4 deiminates 14 of 19 arginyl residues, determination of deimination residues, overview
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
PAD2
-
-
ir
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
-
-
?
N-acetyl-L-arginine + H2O
N-acetyl-L-citrulline ethyl ester + NH3
isoform PAD1 shows 160% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
N-acetyl-L-arginine + H2O
N-acetyl-L-citrulline ethyl ester + NH3
isoform PAD3 shows 135% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
N-acetyl-L-arginine-methyl ester + H2O
N-acetyl-L-citrulline-methyl ester + NH3
isoform PAD1 shows 80% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
N-acetyl-L-arginine-methyl ester + H2O
N-acetyl-L-citrulline-methyl ester + NH3
isoform PAD3 shows 125% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
Mus musculus C57BL/6 / 129S
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
Nalpha-benzoyl-L-citrulline + NH3
isoform PAD1 shows 120% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Nalpha-benzoyl-L-arginine + H2O
Nalpha-benzoyl-L-citrulline + NH3
isoform PAD3 shows 70% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Nalpha-benzoyl-L-arginine + H2O
Nalpha-benzoyl-L-citrulline + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
Nalpha-benzoyl-L-citrulline + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine amide + H2O
Nalpha-benzoyl-L-citrulline amide + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine amide + H2O
Nalpha-benzoyl-L-citrulline amide + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
100% activity
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
100% activity
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
100% activity
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
100% activity
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
-
100% activity
-
-
?
Nalpha-benzoyl-L-arginine methyl ester + H2O
Nalpha-benzoyl-L-citrulline methyl ester + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine methyl ester + H2O
Nalpha-benzoyl-L-citrulline methyl ester + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine-amide + H2O
Nalpha-benzoyl-L-citrulline-amide + NH3
isoform PAD1 shows 110% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Nalpha-benzoyl-L-arginine-amide + H2O
Nalpha-benzoyl-L-citrulline-amide + NH3
isoform PAD3 shows 105% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Nalpha-tosyl-L-arginine-methyl ester + H2O
Nalpha-tosyl-L-citrulline-methyl ester + NH3
isoform PAD1 shows 20% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
Nalpha-tosyl-L-arginine-methyl ester + H2O
Nalpha-tosyl-L-citrulline-methyl ester + NH3
isoform PAD3 shows 22% activity compared to Nalpha-benzoyl-L-arginine ethyl ester
-
-
?
PPGFSPFR + H2O
PPGFSPF-citrulline + NH3
peptide derived from bradykinin
-
-
?
PPGFSPFR + H2O
PPGFSPF-citrulline + NH3
-
peptide derived from bradykinin
-
-
?
PPGFSPFR + H2O
PPGFSPF-citrulline + NH3
peptide derived from bradykinin
-
-
?
protein L-Arg + H2O
?
-
C-1, the most unmodified of the components of myelin basic protein, is an excellent substrate for the enzyme, thereby confirming that the origin of the citrulline in myelin basic protein arises by the action of this enzyme
-
-
?
protein L-Arg + H2O
?
-
expression of the enzyme in luminal and glandular epithelia of the uterus is controlled by amount of the steroid hormones estrogen and progesterone
-
-
?
protein L-Arg + H2O
?
-
the ureido group on the citrulline formed by the peptidylarginine deiminase modification functions to unfold proteins due to decrease in net charge, loss of potential ionic bonds, and interference with H bonds
-
-
?
protein L-Arg + H2O
?
-
peptidylarginine deiminase, acting in concert with arginine-specific proteinases from Porphyromonas gingivalis, promotes the growth of the pathogen in the periodontal pocket, initially by enhancing its survivability and then by assisting the organism in its circumvention of host humoral defenses
-
-
?
protein L-Arg + H2O
?
-
all-trans retinoic acid increases peptidylarginine deiminase activity in a newborn rat keratinocyte cell line
-
-
?
protein L-Arg + H2O
?
-
citrullyl residues in the membranous protein of horny cells of the epidermis of newborn rat are formed by the action of epidermal peptidylarginine deiminase
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
bovine S-carboxymethylated prekeratin and myelin
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
peptidyl deiminase type II is the primary enzyme responsible for the conversion of protein bound arginine to citrulline in the central nervous system
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
[NV]-angiotensin II, fibronectin fragment, LHRH, chicken brain peptide, molluscan cardioexxitatory neuropeptide, bradykinin potentiator B, dynorphin A, [VA]-kemptide, neurotensin, bradykinin, K-bradykinin, MK-bradykinin, Y-bradykinin
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
PAD catalyzes the deimination of the guanidino group from peptidylarginine residues of various peptides to produce peptidylcitrulline and ammonia
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
-
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
-
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
citrullination of proteins may exert a specific role in the course of PNS development and repair
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
PAD1
-
-
ir
protein-L-arginine + H2O
protein-L-citrulline + NH3
PAD4 is a transcriptional coregulator that catalyzes the calcium-dependent conversion of specific arginine residues in proteins to citrulline and plays a role in the onset and progression of the chronic autoimmune disorder rheumatoid arthritis
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
posttranslational convertion, PADI4 plays an essential role in immune cell differentiation and apoptosis, ionomycin-inducible PADI4-decreased cell viability and PADI4-enhanced apoptosis, overview
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
Mus musculus C57BL/6 / 129S
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
-
-
ir
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
citrullination of proteins may exert a specific role in the course of PNS development and repair
-
-
?
trichohyalin + H2O
? + NH3
-
deimination of protein-bound Arg residues to citrulline, the substrate has a highly alpha-helical structure, the reaction proceeds slowly to about 25% and can be forced to a maximum of about 65%
-
-
?
trichohyalin-L-arginine + H2O
trichohyalin-L-citrulline + NH3
PAD3, involvement in skin disease
-
-
ir
trichohyalin-L-arginine + H2O
trichohyalin-L-citrulline + NH3
PAD3
-
-
ir
vimentin-L-arginine + H2O
vimentin-L-citrulline + NH3
PAD2, involvement in Alzheimer's disease
-
-
ir
vimentin-L-arginine + H2O
vimentin-L-citrulline + NH3
PAD2
-
-
ir
vimetin L-arginine + H2O
vimentin L-citrulline + NH3
peptidylarginine deiminase 2
-
-
?
vimetin L-arginine + H2O
vimentin L-citrulline + NH3
peptidylarginine deiminase 4
-
-
?
additional information
?
-
-
PAD II not only binds with the beta-amyloid peptides Abeta1-40, Abeta22-35, Abeta17-28,Abeta25-35 and Abeta32-35 but assists in the proteolytic degradation of these peptides with the concomitant formation of insoluble fibrils
-
-
?
additional information
?
-
-
abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of patients with Alzheimer's disease, strongly suggests that peptidylarginine deiminase has an important role in the onset and progression of abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of Alzheimer's disease
-
-
?
additional information
?
-
peptidylarginine deiminase type 4 plays an essential role in pathogenesis of rheumatoid arthritis.Peptidylarginine deiminase type 4 may contribute to the disrupted apoptosis of tumors by caspase-mediated claevage of cytokeratin
-
-
?
additional information
?
-
-
the enzyme catalyzes post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Peptidylarginine deiminase-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development
-
-
?
additional information
?
-
methylated Arg residues are quite poor substrates for full-length PAD4 in vitro, regardless of whether this residue is in the context of a small molecule or a peptide substrate
-
-
?
additional information
?
-
-
methylated Arg residues are quite poor substrates for full-length PAD4 in vitro, regardless of whether this residue is in the context of a small molecule or a peptide substrate
-
-
?
additional information
?
-
PADI3 expression is driven by Sp1/Sp3 and NF-Y binding to the promoter region
-
-
?
additional information
?
-
-
PADI3 expression is driven by Sp1/Sp3 and NF-Y binding to the promoter region
-
-
?
additional information
?
-
-
the enzyme is involved in autoimmune rheumatoid arthritis
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis
-
-
?
additional information
?
-
-
the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
-
-
?
additional information
?
-
the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
-
-
?
additional information
?
-
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, e.g. PAD2 in glaucoma of the optic nerve, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, e.g. PAD2 in glaucoma of the optic nerve, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, e.g. PAD2 in glaucoma of the optic nerve, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, e.g. PAD2 in glaucoma of the optic nerve, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, e.g. PAD2 in glaucoma of the optic nerve, overview
-
-
?
additional information
?
-
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, overview
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6, PADs are involved in diverse diseases, overview
-
-
?
additional information
?
-
-
substrate binding structure, sequence specificity, overview
-
-
?
additional information
?
-
substrate binding structure, sequence specificity, overview
-
-
?
additional information
?
-
-
a methylated lysine residue flanking the targeted arginine influences PAD-4-mediated deimination
-
-
?
additional information
?
-
-
no activity toward PVRAK, DQRTA, DVRIA, and EPRLF
-
-
?
additional information
?
-
-
the binding affinity of autodeiminated PAD4 for p53 and H3 are similar to non-deiminated PAD4. In contrast, the affinity of autodeiminated PAD4 for HDAC1, PRMT1, and Cit H3 is reduced by 3.7, 4.5, and 10fold, respectively. Results suggest that the autodeimination of PAD4 in vivo could affect its functional activity by regulating its ability to interact with binding partners
-
-
?
additional information
?
-
-
possible 14-3-3 protein binding sites in human PAD6 are identified by in silico methods. Two of these sites are confirmed as 14-3-3 binding sites by fluorescence polarization competition and X-ray crystallography
-
-
?
additional information
?
-
nearly no activity with free L-arginine, L-agmatine, histone H3, and histone H4
-
-
?
additional information
?
-
isoform PAD2 appears to favor citrullination of glycine-containing motifs. Distinct hydrophobic motifs are identified for PAD2 citrullination sites predicted to reside within alpha-helical and beta-sheet regions. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
isoform PAD2 appears to favor citrullination of glycine-containing motifs. Distinct hydrophobic motifs are identified for PAD2 citrullination sites predicted to reside within alpha-helical and beta-sheet regions. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
-
isoform PAD2 appears to favor citrullination of glycine-containing motifs. Distinct hydrophobic motifs are identified for PAD2 citrullination sites predicted to reside within alpha-helical and beta-sheet regions. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
isoform PAD4 appears to favor citrullination of glycine-containing motifs. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
isoform PAD4 appears to favor citrullination of glycine-containing motifs. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
-
isoform PAD4 appears to favor citrullination of glycine-containing motifs. There is potential substrate overlap between coil region citrullination and arginine methylation
-
-
?
additional information
?
-
proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. Pressure-induced translational control of PAD2 expression is consistent with a possible role for PAD2 and citrullination in primary open-angle glaucoma
-
-
?
additional information
?
-
-
proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. Pressure-induced translational control of PAD2 expression is consistent with a possible role for PAD2 and citrullination in primary open-angle glaucoma
-
-
?
additional information
?
-
the cortical granule enzyme plays a role in preimplantation embryonic development
-
-
?
additional information
?
-
-
the cortical granule enzyme plays a role in preimplantation embryonic development
-
-
?
additional information
?
-
PAD 6 is essential for oocyte cytoskeletal sheet formation and female fertility, it plays an important role in germ-cell-specific structures in zygote/embryo development, citrullination is a regulator of fertility, overview
-
-
?
additional information
?
-
-
IKKgamma and PAD2 can coimmunoprecipitate in the presence of the Ca2+ ionophore
-
-
?
additional information
?
-
-
does not citrullinate interleukin-1beta
-
-
?
additional information
?
-
-
the enzyme undergoes automodification
-
-
?
additional information
?
-
no substrate: peptide GFSPFRSS
-
-
?
additional information
?
-
no substrates: peptides Arg-Gly-Glu, Met-Arg-Phe, fibrinogen peptide CESSSHHPGIAEFPS-R-GK
-
-
?
additional information
?
-
-
no substrates: peptides Arg-Gly-Glu, Met-Arg-Phe, fibrinogen peptide CESSSHHPGIAEFPS-R-GK
-
-
?
additional information
?
-
-
no substrate: peptide GFSPFRSS
-
-
?
additional information
?
-
no substrate: peptide GFSPFRSS
-
-
?
additional information
?
-
no substrates: peptides Arg-Gly-Glu, Met-Arg-Phe, fibrinogen peptide CESSSHHPGIAEFPS-R-GK
-
-
?
additional information
?
-
-
PAD2 is involved in some processes of neurodegeneration and myelination in the central nervous system
-
-
?
additional information
?
-
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6
-
-
?
additional information
?
-
no activity with free L-arginine, which is converted by EC 1.14.13.39, nitric oxide synthase, the enzyme is not identical with bacterial arginine deiminase, EC 3.5.3.6
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fibrin L-arginine + H2O
fibrin L-citrulline + NH3
-
citrullinated fibrin is a potential antigen of rheumatoid arthritis
-
-
?
fibrinogen-L-arginine + H2O
fibrinogen-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
filaggrin-L-arginine + H2O
filaggrin-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
glial fibrillary acidic protein L-arginine + H2O
glial fibrillary acidic protein L-citrulline + NH3
-
-
-
?
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
PAD2, involvement in Alzheimer's diease
-
-
ir
glycogen phosphorylase b + H2O
?
-
specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP
-
-
?
histone H2A-L-arginine + H2O
histone H2A-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone H3-L-Arg + H2O
histone H3-L-citrulline
-
PADI4 is a histone H3-specific arginine deiminase. Deimination is a mechanism for antagonizing the transcriptional induction mediated by arginine methylation
-
-
?
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone L-arginine + H2O
histone L-citrulline + NH3
-
PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones
-
-
?
trichohyalin-L-arginine + H2O
trichohyalin-L-citrulline + NH3
PAD3, involvement in skin disease
-
-
ir
vimentin-L-arginine + H2O
vimentin-L-citrulline + NH3
PAD2, involvement in Alzheimer's disease
-
-
ir
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
PAD4, involvement in rheumatoid arthritis
-
-
ir
keratin-L-arginine + H2O
keratin-L-citrulline + NH3
PAD2, involvement in psoriasis
-
-
ir
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
PAD2 and PAD4 are involved in the pathogenesis of demyelination diseases such as multiple sclerosis, overview
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
PAD2, involvement in multiple sclerosis
-
-
ir
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
-
-
?
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
-
-
-
?
protein L-Arg + H2O
?
-
C-1, the most unmodified of the components of myelin basic protein, is an excellent substrate for the enzyme, thereby confirming that the origin of the citrulline in myelin basic protein arises by the action of this enzyme
-
-
?
protein L-Arg + H2O
?
-
expression of the enzyme in luminal and glandular epithelia of the uterus is controlled by amount of the steroid hormones estrogen and progesterone
-
-
?
protein L-Arg + H2O
?
-
the ureido group on the citrulline formed by the peptidylarginine deiminase modification functions to unfold proteins due to decrease in net charge, loss of potential ionic bonds, and interference with H bonds
-
-
?
protein L-Arg + H2O
?
-
peptidylarginine deiminase, acting in concert with arginine-specific proteinases from Porphyromonas gingivalis, promotes the growth of the pathogen in the periodontal pocket, initially by enhancing its survivability and then by assisting the organism in its circumvention of host humoral defenses
-
-
?
protein L-Arg + H2O
?
-
all-trans retinoic acid increases peptidylarginine deiminase activity in a newborn rat keratinocyte cell line
-
-
?
protein L-Arg + H2O
?
-
citrullyl residues in the membranous protein of horny cells of the epidermis of newborn rat are formed by the action of epidermal peptidylarginine deiminase
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
peptidyl deiminase type II is the primary enzyme responsible for the conversion of protein bound arginine to citrulline in the central nervous system
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
PAD catalyzes the deimination of the guanidino group from peptidylarginine residues of various peptides to produce peptidylcitrulline and ammonia
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
-
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
-
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
citrullination of proteins may exert a specific role in the course of PNS development and repair
-
-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
PAD1
-
-
ir
protein-L-arginine + H2O
protein-L-citrulline + NH3
PAD4 is a transcriptional coregulator that catalyzes the calcium-dependent conversion of specific arginine residues in proteins to citrulline and plays a role in the onset and progression of the chronic autoimmune disorder rheumatoid arthritis
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protein-L-arginine + H2O
protein-L-citrulline + NH3
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posttranslational convertion, PADI4 plays an essential role in immune cell differentiation and apoptosis, ionomycin-inducible PADI4-decreased cell viability and PADI4-enhanced apoptosis, overview
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protein-L-arginine + H2O
protein-L-citrulline + NH3
-
-
-
ir
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
citrullination of proteins may exert a specific role in the course of PNS development and repair
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additional information
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-
abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of patients with Alzheimer's disease, strongly suggests that peptidylarginine deiminase has an important role in the onset and progression of abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of Alzheimer's disease
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additional information
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peptidylarginine deiminase type 4 plays an essential role in pathogenesis of rheumatoid arthritis.Peptidylarginine deiminase type 4 may contribute to the disrupted apoptosis of tumors by caspase-mediated claevage of cytokeratin
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additional information
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the enzyme catalyzes post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Peptidylarginine deiminase-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
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additional information
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the enzyme is involved in autoimmune rheumatoid arthritis, isozyme PAD2 is also implicated in neurological diseases with or without ocular manifestations, e.g. multiple sclerosis, autoimmune encephalomyelitis, Alzheimer's disease, and glaucoma
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additional information
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a methylated lysine residue flanking the targeted arginine influences PAD-4-mediated deimination
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additional information
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the binding affinity of autodeiminated PAD4 for p53 and H3 are similar to non-deiminated PAD4. In contrast, the affinity of autodeiminated PAD4 for HDAC1, PRMT1, and Cit H3 is reduced by 3.7, 4.5, and 10fold, respectively. Results suggest that the autodeimination of PAD4 in vivo could affect its functional activity by regulating its ability to interact with binding partners
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additional information
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proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. Pressure-induced translational control of PAD2 expression is consistent with a possible role for PAD2 and citrullination in primary open-angle glaucoma
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additional information
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proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. Pressure-induced translational control of PAD2 expression is consistent with a possible role for PAD2 and citrullination in primary open-angle glaucoma
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additional information
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the cortical granule enzyme plays a role in preimplantation embryonic development
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additional information
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the cortical granule enzyme plays a role in preimplantation embryonic development
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additional information
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PAD 6 is essential for oocyte cytoskeletal sheet formation and female fertility, it plays an important role in germ-cell-specific structures in zygote/embryo development, citrullination is a regulator of fertility, overview
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additional information
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IKKgamma and PAD2 can coimmunoprecipitate in the presence of the Ca2+ ionophore
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additional information
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PAD2 is involved in some processes of neurodegeneration and myelination in the central nervous system
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
Ba2+ activates isozymes PAD 1 and 3 to about 15% and 2.5%, respectively, of the level of Ca2+
Ca2+
additional information
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little to no activity is observed with Mg2+, Mn2+, Zn2+ even after long incubation times (up to 2 h)
Ca2+
1 mM required for maximal deimination of filaggrin, peptidylarginine deiminase 1. Maximal deamination of benzoyl-L-Arg ethyl ester at 4 mM or above
Ca2+
1.5 mM required for maximal deimination of filaggrin, peptidylarginine deiminase 3, maximal deimination of benzoyl-L-Arg ethyl ester at 4 mM or above
Ca2+
2.5 mM required for maximal deamination of filaggrin, peptidylarginine deiminase 2. Maximal deimination of benzoyl-L-Arg ethyl ester at 4 mM or above
Ca2+
PAD4 activity is highly specific for calcium. Calcium activation of PAD4 catalysis exhibits positive cooperativity. ca2+ causes conformational change
Ca2+
peptidylarginine deiminase 2 is activated only when sufficient Ca2+ is available (0.01 mM/l), at high concentrations that are normally not present in living cells
Ca2+
required for activity, calcium increases the expression of PAD1 and PAD2
Ca2+
Ca2+ is not only the indispensable factor in the environment of deimination reaction, but is also considered as a major regulator of PAD genes at the transcriptional level
Ca2+
-
dependent on, phoshatidylserine and phosphatidylcholine reduce the Ca2+-dependence by almost 2fold
Ca2+
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dependent on, the concentration of calcium required for half-maximal activity is in the mid to high micromolar range
Ca2+
-
high concentrations of Ca2+ (more than 0.1 mM) are required for activity, the enzyme has 5 Ca2+ binding sites
Ca2+
dependent on, the concentration of calcium that is required for half-maximal activity is 0.2 mM
Ca2+
absolutely required, K0.5 value 0.18 mM. The enzyme binds calcium in a stepwise fashion
Ca2+
the concentration of calcium required for in vitro activity is at least 10 times higher than cellular calcium concentrations (i.e., 0.0001-0.010 mM). Calcium binding occurs in an ordered fashion. A calcium switch (calcium binding sites 3, 4, and 5) controls the overall calcium dependence of the enzyme
Ca2+
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half-maximal activity: 2 mM for peptidyl arginine deiminase I and 4 mM for peptidyl arginine deiminase III
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-3-[2-[4-(2-carbamimidamidoethyl)-1H-1,2,3-triazol-1-yl]acetamido]-3-(4-fluorophenyl)propanoic acid
1,2,3-triazole peptidomimetic-based compound, 39% inhibition at 1 microM, 99% inhibition at 10 microM
(3S)-3-[2-[4-(2-carbamimidamidoethyl)-1H-1,2,3-triazol-1-yl]acetamido]-3-phenylpropanoic acid
1,2,3-triazole peptidomimetic-based compound, 26% inhibition at 1 microM, 69% inhibition at 10 microM
1-(2-{4-[(aminooxy)sulfinyl]phenyl}ethyl)guanidine hydrochloride
5% inhibition at 0.01 mM
1-[3-(1H-imidazol-4-yl)propyl]-3-{2-[(4-phenyl-1,2,5-oxadiazol-3-yl)oxy]ethyl}guanidine hydrochloride
34% inhibition at 0.01 mM
1-[[6-amino-5-(benzoylamino)-6-oxohexyl]amino]-2-chloroethaniminium
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potent, irreversible and specific PAD3 inhibitor
1-[[6-amino-5-(benzoylamino)-6-oxohexyl]amino]-2-fluoroethaniminium
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potent, irreversible and specific PAD3 inhibitor
2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
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2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
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2-chloro-N-[3-(2,5-dioxo-1-phenylimidazolidin-4-yl)propyl]ethanimidamide
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2-cyano-1-methyl-3-(2-{[(5-methyl-1H-imidazol-4-yl)methyl]sulfanyl}ethyl)guanidine
1% inhibition at 0.01 mM
2-cyano-1-{2-[({2-[(diaminomethylidene)amino]-1,3-thiazol-5-yl}methyl)sulfanyl]ethyl}-3-(2-hydroxyethyl)guanidine ethanedioate
3% inhibition at 0.01 mM
2-{[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]carbamoyl}benzoic acid
15fold selectivity versus PAD2 and PAD3; 15fold selectivity versus PAD2 and PAD3; 15fold selectivity versus PAD2 and PAD3; 15fold selectivity versus PAD2 and PAD3
2-{[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]carbamoyl}benzoic acid
exhibits 20 to 30fold selectivity over isoform PAD2 and PAD3 when compared to PAD1; exhibits 20 to 30fold selectivity over isoform PAD2 and PAD3 when compared to PAD1; exhibits 20 to 30fold selectivity over isoform PAD2 and PAD3 when compared to PAD1; exhibits 20 to 30fold selectivity over isoform PAD2 and PAD3 when compared to PAD1
4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-2-ethoxy-N-(4-methoxyphenyl)benzamide
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4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-2-methoxy-N-(4-methoxyphenyl)benzamide
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4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-N-(4-methoxyphenyl)benzamide
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4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-N-phenylbenzamide
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chloro-N-(3-{1-[(2'-chloro-3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
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chloro-N-(3-{1-[(2'-chloro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
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chloro-N-(3-{1-[(3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
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H2O2
in vitro inhibitory to isoform Pad2 above 0.04 mM, peptidylarginine deiminase released from stimulated leukocytes is unaffected by exogenously added H2O2 at concentrations up to 1000 microM; in vitro inhibitory to isoform Pad4 above 0.04 mM, peptidylarginine deiminase released from stimulated leukocytes is unaffected by exogenously added H2O2 at concentrations up to 1000 microM
lipid vesicle
binding of substrate myelin basic protein to lipid vesicles, consisting of 7.8% phosphatidylserine and 92.2% phosphatidylcholine, increases deimination activity, but in the 40 mino acid C-terminal region, where the arginyl residues are no longer deiminated, while they are deiminated in aqueous solution; binding of substrate myelin basic protein to lipid vesicles, consisting of 7.8% phosphatidylserine and 92.2% phosphatidylcholine, increases deimination activity, but in the 40 mino acid C-terminal region, where the arginyl residues are no longer deiminated, while they are deiminated in aqueous solution
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N-(3-{1-[([1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)(chloro)ethanimidamide
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N-alpha-benzoyl-N5-(2-fluoro-1-iminoethyl)-L-ornithine amide
i.e. F-amidine, a potent and bioavailable irreversible inactivator of PAD4, structure of the PAD4-F-amidine-calcium complex, overview
N-[(1R)-1-(biphenyl-3-yl)ethyl]-4-[(2-chloroethanimidoyl)amino]butanamide
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N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl]benzamide
preferentially inhibits protein-arginine deiminase 2 by 3fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases
N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl][1,1'-biphenyl]-4-carboxamide
preferentially inhibits protein-arginine deiminase 2 by 25fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases
N-[(1S)-1-(biphenyl-3-yl)ethyl]-4-[(2-chloroethanimidoyl)amino]butanamide
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N-[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
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N-[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
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N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
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N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
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N-[(3'-bromobiphenyl-3-yl)methyl]-4-[(2-chloroethanimidoyl)amino]butanamide
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N-[([1,1'-biphenyl]-3-yl)methyl]-4-[(2-chloroethanimidoyl)amino]butanamide
inhibitor at at 10 microM rescues thapsigargin-induced cell death in HEK293T cells
N-[3-(1H-imidazol-4-yl)propyl]-N'-{3-[(5-oxo-4-phenyl-1,2lambda~5~,5-oxadiazol-3-yl)oxy]propyl}guanidine hydrochloride
36% inhibition at 0.01 mM
N-[3-[5-([1,1'-biphenyl]-3-yl)-1H-imidazol-2-yl]propyl](chloro)ethanimidamide
inhibitor at at 10 microM rescues thapsigargin-induced cell death in HEK293T cells
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}benzamide
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N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}[1,1'-biphenyl]-4-carboxamide
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N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}benzamide
highly selective isoform PAD2 inhibitor; highly selective isoform PAD2 inhibitor; highly selective isoform PAD2 inhibitor; highly selective isoform PAD2 inhibitor
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}[1,1'-biphenyl]-4-carboxamide
preferentially inhibits isoform PAD2 by 3 to 25fold with the highest selectivity being observed for PAD2 over PAD4; preferentially inhibits isoform PAD2 by 3 to 25fold with the highest selectivity being observed for PAD2 over PAD4; preferentially inhibits isoform PAD2 by 3 to 25fold with the highest selectivity being observed for PAD2 over PAD4; preferentially inhibits isoform PAD2 by 3 to 25fold with the highest selectivity being observed for PAD2 over PAD4
N2-benzoyl-N5-(N,N-dimethylcarbamimidoyl)-L-ornithine
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inhibits PAD4 at high micromolar to millimolar concentrations
oxalic acid 3-(N''-cyano-N'-{2-[({2-[(diaminomethylidene)amino]-1,3-thiazol-5-yl}methyl)sulfanyl]ethyl}carbamimidamido)propane-1,2-diyl dinitrate
8% inhibition at 0.01 mM
oxalic acid 3-(N''-cyano-N'-{2-[({2-[(diaminomethylidene)amino]-1,3-thiazol-5-yl}methyl)sulfanyl]ethyl}carbamimidamido)propyl nitrate
10% inhibition at 0.01 mM
oxalic acid 3-({2-[({5-[(dimethylamino)methyl]furan-2-yl}methyl)sulfanyl]ethyl}amino)-4-(methylamino)-1H-1lambda~4~,2,5-thiadiazol-1-one
9% inhibition at 0.01 mM
2-chloroacetamidine
inhibits PAD4, inactivates covalent modification on Cys645
Cl-amidine
inhibits PAD4, inactivates covalent modification on Cys645
Cl-amidine
inhibits PAD4 by covalent modification Cys-645 at the active site of the enzyme, Cl-amidine inhibits more than 50% of the PAD4 activity at the 0.05 mM concentration, whereas over 90% inhibition is reached with 0.2 mM
Cl-amidine
-
inactivates isozyme PAD4 by the covalent modification of an active-site cysteine that is critical for catalysis
Cl-amidine
-
highly potent PAD4 inactivator, inactivates the enzyme via the alkylation of Cys645
Cl-amidine
inhibitor binds covalently to the catalytic C351-Sgamma atom, mimicking a reaction intermediate
F-amidine
inhibits PAD4, inactivates covalent modification on Cys645
F-amidine
-
inactivates isozyme PAD4 by the covalent modification of an active-site cysteine that is critical for catalysis
F-amidine
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highly potent PAD4 inactivator, inactivates the enzyme via the alkylation of Cys645
iodoacetamide
-
PAD exhibits pseudo first-order loss of activity in the presence of 0.1-10 mM iodoacetamide. When substrate (0.8 mM N-alpha-benzoyl-L-arginine) is present in the inactivation reaction, PAD retains 88% activity after a 4 min incubation, compared to only 32% residual activity under the same reaction conditions in the absence of substrate
iodoacetate
-
PAD exhibits pseudo first-order loss of activity in the presence of 0.5-20 mM iodoacetate
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide
i.e. Cl-amidine, a PAD4 inactivator with enhanced potency
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine ethyl ester
complete inhibition of recombinant PAD4 at 2 mM
paclitaxel
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complete inhibition of amidine hydrolysis of benzoyl-Arg ethyl ester by 12.5 mM, complete inhibition of amidine hydrolysis of myelin basic protein by 0.5 mM, non-competitive
additional information
IC50 values for amidine derivatives, overview, inhibition mechanism and structure-activity relationships, overview
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additional information
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PAD4 inhibitor screening based on a PAD4-targeted activity-based protein profiling reagent, denoted rhodamine-conjugated F-amidine, RFA, rapid competitive assay method development, overview
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additional information
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methylated Arg derivatives are very poor or inactive inhibitors of PAD4
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additional information
methylated Arg derivatives are very poor or inactive inhibitors of PAD4
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additional information
methylated Arg derivatives are very poor or inactive inhibitors of PAD4
-
additional information
methylated Arg derivatives are very poor or inactive inhibitors of PAD4
-
additional information
methylated Arg derivatives are very poor or inactive inhibitors of PAD4
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additional information
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the methyl ester side chain of paclitaxel alone does not inhibit activity of PAD2
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additional information
development of furan-containing inhibitors based on peptide KSIRDTP and molecular docking studies. Inhibitors act reversibly and competitively
-
additional information
-
substrate protects the enzyme from inactivation
-
additional information
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1 mM tosyl phenylalanyl chloromethyl ketone and 0.043 mM leupeptin do not inhibit enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrogen carbonate
physiological levels of hydrogen carbonate upregulate citrullination by recombinant PAD2/4 and endogenous PADs in neutrophils. The impact of hydrogen carbonate is independent of calcium and pH
lipid vesicle
binding of substrate myelin basic protein to lipid vesicles, consisting of 7.8% phosphatidylserine and 92.2% phosphatidylcholine, increases deimination activity, but in the 40 amino acid residue C-terminal region, where the arginyl residues are no longer deiminated, while they are deiminated in aqueous solution
-
additional information
overexpression of PAD2 increases expression of PAD4 but not other PAD enzymes
-
additional information
overexpression of PAD2 increases expression of PAD4 but not other PAD enzymes
-
additional information
overexpression of PAD2 increases expression of PAD4 enzyme
-
additional information
overexpression of PAD2 increases expression of PAD4 enzyme
-
additional information
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smoking increases peptidylarginine deiminase 2 enzyme expression in human lungs and increases citrullination in BAL cells
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44 - 1.75
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
0.58
Ac-Ser-Gly-Arg-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.15 - 1.07
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
0.37
Ac-Ser-Gly-Arg-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.86
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.17 - 0.34
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
0.43 - 0.66
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
1.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.48 - 2.16
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
0.21 - 0.64
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
0.48 - 3.27
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
0.14
histone H4-L-arginine
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.11
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.18
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.32
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.36
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.3
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.95
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.69
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.8
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.44
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.75
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.15
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.59
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.07
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.16
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.58
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.17
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.34
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.43
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.66
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.15
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.2
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.59
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.22
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.52
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.95
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.48
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.16
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.21
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.42
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.64
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.48
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.86
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.27
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.19
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
3.73
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 2
66.3
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
0.73
benzoyl-Arg-ethyl ester
-
pH 7.6, 37°C, hPADI2 expressed in Escherichia coli
0.91
benzoyl-Arg-ethyl ester
-
pH 7.6, 37°C, hPADI4 expressed in Escherichia coli
0.63
benzoyl-Arg-methyl ester
-
pH 7.6, 37°C, hPADI4 expressed in Escherichia coli
1.97
benzoyl-Arg-methyl ester
-
pH 7.6, 37°C, hPADI2 expressed in Escherichia coli
0.35
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
0.5
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 2
7.5
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
0.16
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.25
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
13.9
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
17.5
N-alpha-benzoyl-L-arginine amide
-
mutant PAD3 enzyme G374R, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.1
N-alpha-benzoyl-L-arginine ethyl ester
mutant F221A/F222A, pH 7.6, 37°C
0.1
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme F221A/F222A
0.12
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D123N
0.14
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D125A
0.16
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, wild-type enzyme
0.19
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.25
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D169A
0.33
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D166A
0.6
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D389A
1.36
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D177A
3.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E352A
4.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme R347
5
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D370A
6.3
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme Q350A
8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D374A
13
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E412A
30
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme W373A
0.37
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.66
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
10.8
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.48
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.46
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.98
Ac-Ser-Gly-Arg-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.57 - 1.08
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
0.93
Ac-Ser-Gly-Arg-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.83
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.77
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.87
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.83
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.31 - 3.39
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
0.34 - 0.56
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
0.21
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.59
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.62
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.13
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.57
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.08
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.75
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.53
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.08
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.6
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.64
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.29
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.92
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.31
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.81
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.39
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.34
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.56
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.057 - 0.65
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
1.93
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
6.22
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 2
11.28
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
0.057 - 0.65
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
0.55
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 2
1.73
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
11.31
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 1
15.24
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 2
1.85
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.1
N-alpha-benzoyl-L-arginine amide
-
mutant PAD3 enzyme G374R, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.76
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.57
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.03
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme Q350A
0.1
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E412A
0.2
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme W373A
0.25
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E352A
0.27
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.35
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D166A
0.51
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D389A
0.6
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D370A
0.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D123N
0.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D125A
1.53
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme R347
1.55
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D374A
1.8
N-alpha-benzoyl-L-arginine ethyl ester
mutant F221A/F222A, pH 7.6, 37°C
1.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D169A
1.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme F221A/F222A
2.65
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, wild-type enzyme
2.65
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D177A
5.94
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.26
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.85
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
5.57
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01 - 3.3
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
1.8 - 3.9
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
1 - 19
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
0.7 - 14
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
0.3 - 2.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val
0.001 - 3.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
0.7 - 5.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
0.4 - 1.2
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
0.2
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.2
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
5.7
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.001
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
kcat_Km value less than 0.001 mM-1*sec-1, isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.4
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.4
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.22
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.5
Ac-Ala-Gly-Arg-Gly-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.9
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.4
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
5.8
Ac-Ser-Ala-Arg-Gly-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.01
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.58
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.3
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.08
Ac-Ser-Gly-Arg-Ala-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.7
Ac-Ser-Gly-Arg-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
6.6
Ac-Ser-Gly-Arg-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.8
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.4
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.9
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.05
Ac-Ser-Gly-Arg-Gly-Ala
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.5
Ac-Ser-Gly-Arg-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
16
Ac-Ser-Gly-Arg-Gly-Ala
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.001
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
-
kcat_Km value less than 0.001 mM-1*sec-1, isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.085
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.6
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
19
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
14
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.5
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.1
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.9
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.6
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
2.5
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.001
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
kcat_Km value less than 0.001 mM-1*sec-1, isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.7
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
5.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.5
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.2
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Lys-His-Lys-Ala-Val
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.7
histone H4-L-arginine
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.3
histone H4-L-arginine
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
9
histone H4-L-arginine
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.13
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
11
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
22
N-alpha-benzoyl-L-arginine amide
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
120000
N-alpha-benzoyl-L-arginine amide
-
mutant PAD3 enzyme G374R, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.005
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme Q350A
0.007
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E412A
0.007
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme W373A
0.025
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.075
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E352A
0.115
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D370A
0.195
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D374A
0.35
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme R347
0.845
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D389A
1.065
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D166A
1.1
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D177A
1.5
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
4.4
N-alpha-benzoyl-L-arginine ethyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
6
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D125A
6.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D123N
7.9
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D169A
16.5
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, wild-type enzyme
18
N-alpha-benzoyl-L-arginine ethyl ester
mutant F221A/F222A, pH 7.6, 37°C
18
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme F221A/F222A
13800
N-alpha-benzoyl-L-arginine ethyl ester
-
mutant PAD3 enzyme G374R, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.12
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
3.3
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
10.4
N-alpha-benzoyl-L-arginine methyl ester
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
2-chloroacetamidine
-
IC50 above 0.5 mM, in 100 mM Tris-HCl (pH 7.6), CaCl2 (10 mM), dithiothreitol (5 mM), at 37°C
0.18
Cl-amidine
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
0.33
F-amidine
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028 - 0.026
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-chloroethaniminium
0.0243 - 0.157
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-fluoroethaniminium
0.5
2-chloroacetamidine
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl (pH 7.6), CaCl2 (10 mM), dithiothreitol (5 mM), at 37°C
0.1
chlortetracycline
Homo sapiens
-
in 100 mM Tris-HCl (pH 7.6), CaCl2 (10 mM), dithiothreitol (2 mM) and NaCl (50 mM) at 37°C
0.5
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine ethyl ester
Homo sapiens
recombinant PAD4, pH 7.6, 37°C
0.0058
N-[([1,1'-biphenyl]-3-yl)methyl]-4-[(2-chloroethanimidoyl)amino]butanamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0054
N-[3-[5-([1,1'-biphenyl]-3-yl)-1H-imidazol-2-yl]propyl](chloro)ethanimidamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0074
N-{(2S)-1-amino-5-[(2-chloroethanimidoyl)amino]-1-oxopentan-2-yl}benzamide
Homo sapiens
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
0.024
N-{(2S)-1-amino-5-[(2-fluoroethanimidoyl)amino]-1-oxopentan-2-yl}benzamide
Homo sapiens
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
0.4
N2-benzoyl-N5-(N,N-dimethylcarbamimidoyl)-L-ornithine
Homo sapiens
-
in 100 mM Tris-HCl (pH 7.6), CaCl2 (10 mM), dithiothreitol (1 mM), at 37°C
5
paclitaxel
Homo sapiens
-
IC50 is about 5 mM, at 52°C for 30 min in 50 mM HEPES (pH 7.6), CaCl2 (5 mM), dithiothreitol (2 mM)
0.78
tetracycline
Homo sapiens
-
in 100 mM Tris-HCl (pH 7.6), CaCl2 (10 mM), dithiothreitol (2 mM) and NaCl (50 mM) at 37°C
0.0028
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-chloroethaniminium
Homo sapiens
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.0041
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-chloroethaniminium
Homo sapiens
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.026
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-chloroethaniminium
Homo sapiens
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.0243
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-fluoroethaniminium
Homo sapiens
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.04
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-fluoroethaniminium
Homo sapiens
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.157
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-fluoroethaniminium
Homo sapiens
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.0008
Cl-amidine
Homo sapiens
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.0062
Cl-amidine
Homo sapiens
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.022
Cl-amidine
Homo sapiens
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
0.0216
F-amidine
Homo sapiens
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.022
F-amidine
Homo sapiens
-
in 100 mM HEPES (pH 7.6), CaCl2 (10 mM), TCEP (0.5 mM), NaCl (50 mM), temperature not specified in the publication
0.0295
F-amidine
Homo sapiens
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.35
F-amidine
Homo sapiens
-
isozyme PAD3, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.434
substrate: benzoyl-L-Arg ethyl ester, 55°C, peptidylarginine deiminase 2
0.583
substrate: benzoyl-L-Arg ethyl ester, 55°C, peptidylarginine deiminase 1
additional information
additional information
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
additional information
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
additional information
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, overview
additional information
-
development and evaluation of a highly sensitive antibody-based assay method for PAD activity determination, calibration using PAD from rabbit skeletal muscle, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
7.4
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 8.9
6 - 10
-
pH 6.0: about 75% of maximal activity, pH 10.0: about 50% of maximal activity, hPADI2
6.5 - 8
pH 6.5: about 50% of maximal activity, pH 8.0: about 70% of maximal activity
6.5 - 9
-
pH 6.5: about 70% of maximal activity, pH 9.0: about 50% of maximal activity, hPADI4
7 - 11
-
pH 7.0: about 45% of maximal activity, pH 11.0: about 40% of maximal activity
5.2 - 8.9
pH 5.2: about 60% of maximal activity, pH 8.9: about 85% of maximal activity, deamination of fillagrin, peptidylarginine deiminase 1
5.2 - 8.9
pH 5.2: about 70% of maximal activity, pH 8.9: about 50% of maximal activity, deimination of fillagrin, peptidylarginine deiminase 3
5.2 - 8.9
pH 5.2: about 70% of maximal activity, pH 8.9: about 75% of maximal activity, deimination of fillagrin, peptidylarginine deiminase 2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
peptidylarginine deiminase 2, patients with rheumatoid arthitis and healthy controls
SwissProt
brenda
peptidylarginine deiminase 4, patients with rheumatoid arthitis and healthy controls
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strong expression by adenocarconoma from colon, gall bladder, lung, pancreas, thyroid, uterus, prostate, stomach, parotid, rectum, ovary, esophagus and duodenum, strong expression. Moderate expression by adenocarcinoma from small intestine
brenda
-
PADI4 is significantly overexpressed in blood of rheumatoid arthritis. Genetic variation within PADI4 is not a major risk factor for rheumatoid arzhritis in Caucasians
brenda
-
in adult mainly expressed in ovary and peripheral blood leukocytes
brenda
peptidylarginine deiminase type 4 is initially expressed in CD34+ cells of bone marrow and then distributed in derives of the multi-potent progenitor cells in diverse tissues
brenda
-
high abundance of PADI14 in the synovial membrane is a prominent feature of rheumatoid arthritis
brenda
-
the level of the enzyme in theses cells decreases as the cells differentiate
brenda
additional information
pressure-treated astrocytes exhibit elevated PAD2 and citrullination without apparent change in PAD2 mRNA
brenda
PAD2 immunoreactivity is increased in Scrapie-infected brains, with staining detected primarily in reactive astrocytes
brenda
-
abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of patients with Alzheimer's disease
brenda
expression levels of PAD2 protein as well as its enzyme activity are significantly increased in brain sections of Scrapie-infected mice, including hippocampus, brain stem, and striatum
brenda
-
embryonal, isozyme expression analysis, PAD2 expression occurs also in 19- to 21-day-old embryos at a developmental stage well before myelination begins, overview
brenda
expression of isoform PAD3 is restricted to granular layer and lower stratum corneum
brenda
isoform PAD1 is detected in all layers of the epidermis, including the stratum corneum
brenda
isoform PAD2 is mainly detected in both the spinous and granular layers with a more intense staining of the latter
brenda
isoform PAD3 expression is restricted to the granular layer and lower stratum corneum
brenda
PAD1 is detected in the entire epidermis with an increasing intensity gradient from the basal to the granular layer
brenda
anagen hair follicle, PAD1 is present in non-cornified Huxley layer, cornified Huxley layer, non-cornified inner root sheath cuticle, companion layer and arrector pili muscles
brenda
anagen hair follicle, PAD2 is present in arrector pili muscles
brenda
anagen hair follicle, PAD3 is present in non-cornified Henle layer, non-cornified Huxley layer, non-cornified inner root sheath cuticle and medulla
brenda
inner root sheath and cuticle of the hair follicles
brenda
-
abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of patients with Alzheimer's disease
brenda
-
embryonal, in the prospective dentate gyrus, microglial marker-negative cells show expression of PAD isozyme 2, but not of isozymes PAD1,3, and 4, overview
brenda
expression of isoform PAD2 in all layers of living keratinocytes with a gradient of expression increasing from the basal (very low detection) to the granular layer, where the protein is located at the cell periphery
brenda
epidermal, isozyme PAD1, PAD1 and MFZ1 increase both during differentiation
brenda
peptidylarginine deiminase 2, cell from patients with rheumatoid arthitis and healthy controls show identical expression patterns
brenda
peptidylarginine deiminase 2, cell from patients with rheumatoid arthitis and healthy controls show identical expression patterns
brenda
peptidylarginine deiminase 4, cell from patients with rheumatoid arthitis and healthy controls show identical expression patterns
brenda
-
quantitative determination of PAD2 and PAD4 by immunohistochemistry
brenda
-
Pad6 mRNA expression is localized to oocytes from primordial through antral follicles, but excluded from granulosa cells, theca cells, and corpora lutea
brenda
glaucomatous, increased expression of PAD2
brenda
from older, glaucomatous DBA/2J mice (primary open-angle glaucoma), but not in younger DGB/2J or control C57BL6J mice
brenda
-
in adult mainly expressed in ovary and peripheral blood leukocytes
brenda
majority of PAD2 staining in immature cell stages, overview
brenda
-
majority of PAD2 staining in immature cell stages, overview
brenda
isoform PAD3 is expressed in granular level of stratum corneum
brenda
PAD1 is present in secretory cells and myoepithelial cells
brenda
PAD2 is present in secretory cells and myoepithelial cells
brenda
-
ovariectomized, amount of the enzyme in the uterus is considerably diminished by ovariectomy, the expression of the enzyme in luminal andd glandular epithelia is controlled by the amount of the steroid hormones estrogen and progesterone
brenda
additional information
isoform PAD2 protein is not detected in lung, heart, liver, granular stomach, and gizzard
brenda
additional information
isoform PAD2 protein is not detected in lung, heart, liver, granular stomach, and gizzard
brenda
additional information
isoform PAD2 protein is not detected in lung, heart, liver, granular stomach, and gizzard
brenda
additional information
-
isoform PAD2 protein is not detected in lung, heart, liver, granular stomach, and gizzard
brenda
additional information
-
PAD3 is not detected in sebaceous gland and sweat gland
brenda
additional information
PAD3 is not detected in sebaceous gland and sweat gland
brenda
additional information
PAD3 is not detected in sebaceous gland and sweat gland
brenda
additional information
PAD2 is expressed in most tissues and cell types
brenda
additional information
PAD2 is expressed in most tissues and cell types
brenda
additional information
-
PAD2 is expressed in most tissues and cell types
brenda
additional information
-
tissue distribution, no activity in testis and liver, overview
brenda
additional information
-
no activity detected in spleen, stomach, small intestine, large intestine, pancreas, serum and heart
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
90% of the deiminase activity is cell- or membrane vesicle-associated
-
brenda
-
90% of enzyme activity is cell surface associated
brenda
-
90% of enzyme activity is cell surface associated
-
brenda
-
during encystation ADI translocates from the cytoplasm to the nucleus
brenda
-
10% of enzyme activity is cytoplasn associated
brenda
-
10% of enzyme activity is cytoplasn associated
-
brenda
-
PAD4 primarily localizes in the cytoplasm in pig oocytes and parthenogenetic embryos
brenda
-
during encystation ADI translocates from the cytoplasm to the nucleus
brenda
PAD4 contains nuclear localization signal region in the subdomain 1
brenda
PAD4 associated with chromatin and with intermediate filaments in the axon
brenda
-
in mouse in vitro fertilized embryos, nuclear translocation starts from the 2-cell stage and gradually increases up to blastocyst
brenda
-
PAD4 associated with chromatin and with intermediate filaments in the axon
-
brenda
-
nuclear translocation of PAD4 is observed in late germinal vesicle stage oocytes prior to germinal vesicle breakdown and is localized around the metaphase (M)I and II spindle. Nucleus-localized PAD4 is noticed partially in blastocysts
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
overexpressing PAD2 reduces LPS-mediated COX-2 up-regulation by 50%. PAD2 overexpression also reduces NF-kappaB activity
malfunction
calcium-dependent histone-modifying enzymes whose activity is dysregulated in inflammatory diseases and cancer
metabolism
protein arginine deiminases are calcium-dependent histone-modifying enzymes whose activity is dysregulated in inflammatory diseases and cancer. PAD2 functions as an estrogen receptor (ER) coactivator in breast cancer cells via the citrullination of histone tail arginine residues at ER binding sites
metabolism
the enzyme mediates histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular traps
physiological function
-
despite PAD2's normally inactive status, it becomes active and citrullinates cellular proteins, but only when the intracellular Ca2+ balance is upset during neurodegenerative changes. Abnormal protein citrullination by PAD2 is closely associated with the pathogenesis of neurodegenerative disorders such as Alzheimers disease and prion disease
physiological function
-
PAD2 plays a regulatory role in the expression of lactation related genes via histone citrullination during diestrus
physiological function
-
PAD4 is involved in cellular differentiation, is a transcriptional corepressor for the estrogen receptor and p53 (deiminates the GRIP1 (glutamate receptor interacting protein 1) binding domain of p300, facilitating its interaction with GRIP1 and thus activating transcription), and is participated in NET formation. PAD4 influences gene expression through the deimination of histones H2A, H3 and H4. PAD4 downregulates the expression of p21, a cell cycle inhibitor, as well as PUMA and OKL38 (pregnancy-induced growth inhibitor), which are inducers of apoptosis. Increased PAD4 activity contributes to the onset and progression of rheumatoid arthritis
physiological function
-
incubation of purified PAD2 and IKKgamma proteins in the presence of Ca2+ citrullinate IKKgamma. Results demonstrate that PAD2 interacts with IKKgamma and suppresses NF-kappaB activity
physiological function
-
PAD negatively regulates enolase activity via citrullination and enolase activity is more inactive in patients with with sporadic Creutzfeldt-Jakob disease and Alzheimer's disease than in controls
physiological function
-
PAD negatively regulates enolase activity via citrullination. Thus, PAD-mediated citrullination regulates the diverse physiological activities of enolase
physiological function
-
the target of citrullination is histone protein (H3), not B23. Therefore the presence of PAD4 and citrullinated histone H3 in oocytes and embryos suggests a possible role for PAD4 in preimplantation embryonic development
physiological function
-
the target of citrullination is histone protein (H3), not B23. Therefore the presence of PAD4 and citrullinated histone H3 in oocytes and embryos suggests a possible role for PAD4 in preimplantation embryonic development
physiological function
-
enzyme's presence in inflamed tissue may promote autoimmune reactions by creation of altered host epitopes
physiological function
during catalysis, enzyme undergoes the transformation between protonation state N (both C351 and H236 are neutral) and state I (both residues exist as a thiolate-imidazolium ion pair). State N is calculated to be more stable than state I by 8.46 kcal/mol, and state N can transform to state I via two steps of substrate-assisted proton transfer. Starting from state N, the deamination reaction corresponds to an energy barrier of 18.82 kcal/mol. The deprotonated C351 initiates the nucleophilic attack to the substrate, which is the key step for deamination reaction. Both the deprotonated D238 and H236 can act as the bases to activate the hydrolytic water, which correspond to similar energy barriers ( about 17 kcal/mol)
physiological function
enzyme is important for bacterial adhesion to fungal cells. The level of binding of a Ppad mutant strain is significantly lower than that observed for the wild-type strain. The viability of Porphyromonas gingivalis cells under normoxia increases in the presence of fungal biofilm compared with the bacteria that form single-species biofilm
physiological function
in fetal testes from Sox9 knockout mice, Pai2 expression is greatly reduced. Padi-/- XY mice are fertile and show no apparent reproductive anomalies. No significant difference in H3 citrullination between wildtype and Padi2-/- XY gonads is observed
physiological function
phorbol 12-myristate 13-acetate-stimulated leukocytes citrullinate fibrinogen. The citrullination is markedly enhanced when ROS formation is inhibited by the NADPH oxidase inhibitor diphenyleneiodonium. Peptidylarginine deiminase released from stimulated leukocytes is unaffected by exogenously added H2O2 at concentrations up to 1000 microM
physiological function
-
enzyme is important for bacterial adhesion to fungal cells. The level of binding of a Ppad mutant strain is significantly lower than that observed for the wild-type strain. The viability of Porphyromonas gingivalis cells under normoxia increases in the presence of fungal biofilm compared with the bacteria that form single-species biofilm
-
physiological function
-
during catalysis, enzyme undergoes the transformation between protonation state N (both C351 and H236 are neutral) and state I (both residues exist as a thiolate-imidazolium ion pair). State N is calculated to be more stable than state I by 8.46 kcal/mol, and state N can transform to state I via two steps of substrate-assisted proton transfer. Starting from state N, the deamination reaction corresponds to an energy barrier of 18.82 kcal/mol. The deprotonated C351 initiates the nucleophilic attack to the substrate, which is the key step for deamination reaction. Both the deprotonated D238 and H236 can act as the bases to activate the hydrolytic water, which correspond to similar energy barriers ( about 17 kcal/mol)
-
physiological function
-
enzyme's presence in inflamed tissue may promote autoimmune reactions by creation of altered host epitopes
-
Show AA Sequence and Transmembrane Helices (2099 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60880
-
calculated mass of truncated PAD with its poly-His and Xpress epitope tags
75000
76000
85000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
dimerization of PAD4 is essential for full enzyme activity and calcium-binding cooperativity
monomer
additional information
monomer
-
monomeric PAD4 maintains 25-50% enzyme activity compared to the dimeric enzyme
additional information
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
additional information
-
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
-
the potential Asn-linked glycosylation site, Asn542-Glu543-Ser544 has no carbohydrate moiety
proteolytic modification
-
PAD4 autodeimination does not alter the activity, substrate specificity, or calcium dependence of this isozyme. Six in vitro sites of autodeimination are identified: R123, R156, R205, R419, R484, and R639. Autodeimination of PAD4 reduces protein-protein interactions
side-chain modification
side-chain modification
-
methylation of Arg106 is a naturally occuring modification of the enzyme that affects deimination of Arg residues
side-chain modification
-
methylation of Arg107 is a naturally occuring modification of the enzyme that affects deimination of Arg residues
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
27 structures and calcium-titrations by X-ray crystallography to determine order of binding and affinity for the six calcium ions that bind and activate the enzyme
crystal structures of a Ca2+-bound PAD4 mutant C645A in complex with three histone N-terminal peptides, each consisting of 10 amino acid residues that include one target arginine residue for the enzyme (H3/Arg-8, H3/Arg-17, and H4/Arg-3). hanging-drop vapor-diffusion method
hanging drop vapor diffusion method, using 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350
hanging drop vapor diffusion method, using 20 mM imidazole buffer pH 7.0, 0.2 M Li2SO4, 15% (w/v) polyethylene glycol monomethylether 5000
purified recombinant GST-tagged PAD4 mutant C645A in complex with Ca2+ and histone-derived N-terminal peptide substrates, hanging-drop vapor-diffusion method, soaking of Ca2+-free crystals in crystallization buffer containing 5 mM CaCl2 and each histone N-terminal peptide for 8 h at 20°C, X-ray diffraction structure determination and anaylsis at 2.0-2.225 A resolution, molecular replacement
sitting-drop vapor-diffusion technique at 23°C, apoPAD2 crystals with increasing concentrations of calcium (0-10 mM), 16 structures are solved at eight different calcium concentrations to 1.66-1.97 A
structure of isoform Pad1, in presence of Ca2+, to 3.2 A resolution. The asymmetric unit containes two PAD1 molecules, with an elongated N-terminal loop that appears to prevent the formation of a homodimer. The N-terminal loop occupies the substrate binding site of the adjacent PAD1 molecules in the crystal
structures of wild-type and mutant C351A, to 1.46 and 1.48 A resolution. Catalysis is mediated by residues Asp130, His236, Asp238, Asn297 and Cys351. Arg152 and Arg154 may determine the substrate specificity
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
C645A
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
D370A
D374A
D389A
D465A
residue involved in dimerization, about 30% of wild-type catalytic effciency
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
E352A
E412A
F221A/F222A
F285AV284A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
G374R
-
the PAD3 mutant does not display PAD4-like kinetics with benzoylated arginine derivatives
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
N648A
37% of wild type activity, ligand for water-mediated 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
R372K
R372Q
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
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
W373A
50fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
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
additional information
C645A
site-directed mutagemesis, inactive mutant, substrate-bound structure analysis
D123N
2.5fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D125A
2.75fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D166A
85fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D169A
2fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D177A
15fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D370A
220fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D374A
145fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D389A
20fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E352A
1250fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E412A
3300fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
F221A/F222A
1.1fold increase in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
F221A/F222A
slight increase in activity, mutations do not significantly alter the calcium dependence of the enzyme
Q350A
2350fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
R347A
fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
R372K
-
830fold decreased in kcat/M with either substrate [histone H4]-L-Arg or Nalpha-benzoyl L-arginine ethyl ester
R372Q
-
830fold decreased in kcat/M with either substrate [histone H4]-L-Arg or Nalpha-benzoyl L-arginine ethyl ester
Y435A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 2.33 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 5.9/sec, quaternary structure: monomer, Kd: 30.3 microM
Y435A
residue involved in dimerization, about 4% of wild-type catalytic effciency
additional information
the promoter activity of MFZ1- and Sp1-binding site mutants is reduced, overview
additional information
-
the promoter activity of MFZ1- and Sp1-binding site mutants is reduced, overview
additional information
generation of PAD6-deficient mice, enzyme inactivation affects female, but not male, fertility, it results in dispersal of the cytoskeletal sheets in oocytes, phenotype, overview
additional information
inactivation of PAD2 does not affect PAD4 activity, but leads to limited deimination due to the narrower cleavage spectrum of arginyl residues in myelin basic protein for PAD4, overview
additional information
inactivation of PAD2 does not affect PAD4 activity, but leads to limited deimination due to the narrower cleavage spectrum of arginyl residues in myelin basic protein for PAD4, overview
additional information
-
inactivation of PAD2 does not affect PAD4 activity, but leads to limited deimination due to the narrower cleavage spectrum of arginyl residues in myelin basic protein for PAD4, overview
-
additional information
-
strain T2 shows three amino-acid substitutions directly preceding catalytic residue H236 (G231N/E232T/N235D) when compared with PPAD from the reference strain ATCC 33277. Mutations localize to a loop engaged in substrate/inhibitor binding. Mutation of these positions in the reference strain results in twofold higher cell-associated citrullinating activity. Similar to PPAD-T1, recombinant PPAD-T2 citrullinates arginines at the C-termini of general peptidic substrates but not within peptides
additional information
strain T2 shows three amino-acid substitutions directly preceding catalytic residue H236 (G231N/E232T/N235D) when compared with PPAD from the reference strain ATCC 33277. Mutations localize to a loop engaged in substrate/inhibitor binding. Mutation of these positions in the reference strain results in twofold higher cell-associated citrullinating activity. Similar to PPAD-T1, recombinant PPAD-T2 citrullinates arginines at the C-termini of general peptidic substrates but not within peptides
additional information
-
strain T2 shows three amino-acid substitutions directly preceding catalytic residue H236 (G231N/E232T/N235D) when compared with PPAD from the reference strain ATCC 33277. Mutations localize to a loop engaged in substrate/inhibitor binding. Mutation of these positions in the reference strain results in twofold higher cell-associated citrullinating activity. Similar to PPAD-T1, recombinant PPAD-T2 citrullinates arginines at the C-termini of general peptidic substrates but not within peptides
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
enzyme activity decreases by 13% following exposure of cells to 60°C for 10 min
68
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the PAD2 level is relatively higher for immobilized astrocytes in polyethylene set up compared to astrocytes not subjected to immobilization or in glass bead set up. Elevation in PAD2 and deimination level is observed in astrocytes subjected to mechanical stretching or hydrostatic pressure.
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C, in presence of the stabilizing factors FMN or FAD, at pH 5.5, 7.5 or 9.0, no appreciable loss of activity
-
-80°C, 10% 10 mM Tris-HCl, pH 8.0, 1 mM EDTA, 500 mM NaCl, 1 mM DTT and 10% glycerol, stable for several months
-80°C, in 20 mM Tris-HCl, pH 7.6, 1 mM EDTA, 500 mM NaCl, 0.5M tris(2-carboxyethyl) phosphine, and 10% (v/v) glycerol, several months, the enzyme remains stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag affinity column chromatography and Sephacryl S-200 gel filtration
Ni2+-charged HiTrap column chromatography and Sephacryl S-200 gel filtration
PAD is purified in 12.5% yield and 137fold from bovine brain by chromatography on diethylaminoethyl (DEAE)-sephacel
-
recombinant GST-tagged PAD4 mutant C645A by glutathione affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells as a fusion protein with glutathione S-transferase
-
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli strain BL21(DE3)pLysS, COS-1 and HEK-293 cells
expressed in Escherichia coli strain BL21, HEK-293T, and MCF-7 cell lines
expression analysis
expression in Escherichia coli
gene padi4, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
-
PAD2 and PAD4 from spleen, expression of N-terminally His-tagged enzymes in Escherichia coli strain BL21(DE3)
promoter sequence determination and anaylsis 195 base pairs upstream from the transcription initiation site, primer extension method and determination of minimal promoter sequence, the promoter activity depends on MFZ1 and Sp1/Sp3 binding to their specific sites
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
epidermal growth factor upregulates PAD2 transcription and translation. PAD2 expression varies across the estrous cycle, with expression initiating during mammary gland proliferation in estrus/early diestrus and increasing through lactation during diestrus. PAD2 mRNA and protein levels are highest in alveolar unit epithelium during late diestrus
-
estrogen or progesterone do not upregulate PAD2 transcription and translation
-
PAD immunopositivity in the hepatocytes increases with the stage of hepatic fibrosis. PAD immunopositivity by hepatocytes significantly increases with the increase in the CD38 by the hepatic stellate cells. PAD immunopositivity increases with Metavir activity
-
PAD2 mRNA expression is detected in the brains of mice as early as embryonic day 15, and its expression in cerebral cortex, hippocampus, and cerebellum increases significantly as the animals age from 3 to 30 months old, PAD2 mRNA levels in the cerebral cortex, cerebellum, and hippocampus at 30 months were about 1.6fold,1.5fold, and 1.6fold higher, respectively, than in 3-month-old animals
-
PAD4 is elevated in patients with multiple sclerosis, ankylosing spondylitis, and osteoarthritis, and PAD4 levels are elevated in the blood of patients with malignant cancers
-
peptidylarginine deiminase 6 is downregulated in newborn ovary homeobox-null ovaries
-
SOX9 positively regulates Padi2 transcription and FOXL2 antagonizes it in TM3 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
pharmacology
analysis
adding bicarbonate to commercial peptidyl arginine deiminase activity kits could increase assay performance and biological relevance
analysis
development of a fluorescent probe to detect citrulline with high sensitivity and broad dynamic range and establishment of multiple assay systems for PAD subtypes activities, including PAD2 and PAD4, with the probe
drug development
-
PAD4 is a leading target for the development of a rheumatoid arthritis pharmaceutical
drug development
the enzyme is a particularly attractive therapeutic target for breast cancer because it is recruited by the estrogen receptor to endoplasmic reticulum target gene promoters where it citrullinates histone H3 at R26, leading to ER-target gene activation
medicine
-
PAD4 is a potential therapeutic target for the treatment of rheumatoid arthritis. PAD4 mutations are associated with anti-CCP antibody production and the increased expression of PAD4 in the rheumatoid arthritis synovium
medicine
-
peptidyl arginine deiminase is an immunohistochemical marker for liver fibrosis in patients with chronic hepatitis
medicine
in a a triple-culture system of neutrophils and human dental follicle stem cells primed with Porphyromonas gingivalis, infection of dental follicle stem cells with Porphoyromonas gingivalis prolongs the survival of neutrophils and increases their migration. The phenotypic changes depend on direct cellular contacts and PPAD expression by Porphyromonas gingivalis
medicine
-
in a a triple-culture system of neutrophils and human dental follicle stem cells primed with Porphyromonas gingivalis, infection of dental follicle stem cells with Porphoyromonas gingivalis prolongs the survival of neutrophils and increases their migration. The phenotypic changes depend on direct cellular contacts and PPAD expression by Porphyromonas gingivalis
-
pharmacology
PAD1 is a target in skin diseases including psoriasis
pharmacology
PAD2 is a target for treatment of glaucoma and multiple sclerosis
pharmacology
PAD3 is a target in skin diseases including psoriasis, PAD3-like protein is a target for treatment of certain cancers
pharmacology
PAD4 inhibitors F-and Cl-amidine represent potential lead compounds for the treatment of rheumatoid arthritis because a growing body of evidence supports a role for PAD4 in the onset and progression of this chronic autoimmune disorder
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EXTERNAL LINKS (specific for EC-Number 3.5.3.15)
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Release 2023.1 (January 2023)
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