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Information on EC 3.5.3.15 - protein-arginine deiminase and Organism(s) Homo sapiens and UniProt Accession Q9ULW8

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EC Tree
IUBMB Comments
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9ULW8
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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, peptidylarginine deiminase type 4, protein arginine deiminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptidylarginine deiminase
-
peptidylarginine deiminase 3
-
peptidylarginine deiminase type III
-
protein arginine deiminase 3
-
deiminase, protein (arginine)
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-
-
-
HL-60 PAD
-
-
-
-
hPADI2
-
-
hPADI4
-
-
hPADVI
-
-
PAD 1
-
isozyme
PAD 3
-
isozyme
PAD 4
-
isozyme
PAD-4
-
-
PAD-H19
-
-
-
-
PAD-R11
-
-
-
-
PAD-R4
-
-
-
-
PADI4
peptidyl arginine deiminas 4
-
-
peptidyl arginine deiminase
-
-
peptidylarginine deiminase
peptidylarginine deiminase 1
-
peptidylarginine deiminase 2
peptidylarginine deiminase 4
peptidylarginine deiminase isoform VI
-
-
peptidylarginine deiminase IV
peptidylarginine deiminase type 4
-
Peptidylarginine deiminase type alpha
-
-
-
-
peptidylarginine deiminase type I
-
peptidylarginine deiminase type II
-
peptidylarginine deiminase type VI
-
-
peptidylarginine deiminase-4
-
-
protein arginine deiminase
protein arginine deiminase 2
-
protein arginine deiminase 4
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-L-arginine iminohydrolase
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
CAS REGISTRY NUMBER
COMMENTARY hide
75536-80-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
1-[3-(2,5-dioxoimidazolidin-4-yl)propyl]guanidine + H2O
N-[3-(2,5-dioxoimidazolidin-4-yl)propyl]urea + NH3
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
1-[[6-(benzyloxy)-1H-indol-2-yl]methyl]guanidine + H2O
N-[[6-(benzyloxy)-1H-indol-2-yl]methyl]urea + NH3
show the reaction diagram
-
-
-
?
4-carbamimidamido-N-(diphenylmethyl)butanamide + H2O
4-(carbamoylamino)-N-(diphenylmethyl)butanamide + NH3
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
acetyl-L-Arg methyl ester + H2O
acetyl-L-citrulline methyl ester + NH3
show the reaction diagram
peptidylarginine deiminase 3
-
-
?
benzoyl-L-Arg + H2O
benzoyl-L-citrulline + NH3
show the reaction diagram
peptidylarginine deiminase 3
-
-
?
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
peptidylarginine deiminase 3
-
-
?
filaggrin L-Arg + H2O
filaggrin citrulline + NH3
show the reaction diagram
-
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
show the reaction diagram
keratin L-arginine + H2O
keratin L-citrulline + NH3
show the reaction diagram
peptidylarginine deiminase 3
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
N-(biphenyl-3-ylmethyl)-4-carbamimidamidobutanamide + H2O
N-[([1,1''-biphenyl]-3-yl)methyl]-4-(carbamoylamino)butanamide + NH3
show the reaction diagram
-
-
-
?
N-[(1R)-1-(biphenyl-3-yl)ethyl]-4-carbamimidamidobutanamide + H2O
N-[(1R)-1-([1,1''-biphenyl]-3-yl)ethyl]-4-(carbamoylamino)butanamide + NH3
show the reaction diagram
-
-
-
?
N-[(1S)-1-(biphenyl-3-yl)ethyl]-4-carbamimidamidobutanamide + H2O
N-[(1S)-1-([1,1''-biphenyl]-3-yl)ethyl]-4-(carbamoylamino)butanamide + NH3
show the reaction diagram
-
-
-
?
N-[(3'-bromobiphenyl-3-yl)methyl]-4-carbamimidamidobutanamide + H2O
N-[(3''-bromo[1,1''-biphenyl]-3-yl)methyl]-4-(carbamoylamino)butanamide + NH3
show the reaction diagram
-
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
show the reaction diagram
S100A3-L-arginine + H2O
S100A3-L-citrulline + NH3
show the reaction diagram
-
-
-
?
trichohyalin-L-arginine + H2O
trichohyalin-L-citrulline + NH3
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Ac-Ala-Gly-Arg-Gly-Lys + H2O
Ac-Ala-Gly-Cit-Gly-Lys + NH3
show the reaction diagram
-
-
-
-
?
Ac-Ser-Ala-Arg-Gly-Lys + H2O
Ac-Ser-Ala-Cit-Gly-Lys + NH3
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Ala-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Ala-Lys + H2O
Ac-Ser-Gly-Cit-Ala-Lys + NH3
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-acetyl-Lys-Gly-Gly-acetyl-Lys-Gly-Leu-Gly-acetyl-Lys-Gly-Gly-Ala-acetyl-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Ala + H2O
Ac-Ser-Gly-Cit-Gly-Ala + NH3
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys + H2O
Ac-Ser-Gly-Cit-Gly-Lys + NH3
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Ala-Val + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Ala-Arg-His-Arg-Lys-Val + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Ala-His-Arg-Ala-Val + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Ala-Ala-Val + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
acetyl-L-Arg + H2O
acetyl-L-citrulline + NH3
show the reaction diagram
peptidylarginine deiminase 1
-
-
?
acetyl-L-Arg methyl ester + H2O
acetyl-L-citrulline methyl ester + NH3
show the reaction diagram
benzoyl-Arg + H2O
benzoyl-citrulline + NH3
show the reaction diagram
-
-
-
?
benzoyl-Arg-ethyl ester + H2O
benzoyl-citrulline-ethyl ester + NH3
show the reaction diagram
benzoyl-Arg-methyl ester + H2O
benzoyl-citrulline-methyl ester + NH3
show the reaction diagram
benzoyl-Arg-NH2 + H2O
benzoyl-citrulline-NH2 + NH3
show the reaction diagram
benzoyl-L-Arg + H2O
benzoyl-L-citrulline + NH3
show the reaction diagram
benzoyl-L-Arg ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
benzoyl-L-arginine + H2O
benzoyl-L-citrulline + NH3
show the reaction diagram
-
-
-
?
benzoyl-L-arginine amide + H2O
?
show the reaction diagram
-
best small-molecule substrate for PAD4
-
-
?
benzoyl-L-arginine amide + H2O
benzoyl-L-citrulline amide + NH3
show the reaction diagram
-
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
-
-
-
?
benzoyl-L-arginine methyl ester + H2O
benzoyl-L-citrulline methyl ester + NH3
show the reaction diagram
-
-
-
?
beta-actin L-arginine + H2O
beta-actin L-citrulline + NH3
show the reaction diagram
substrate for isoform PAD2 only
-
-
?
citrullinated histone H3 L-arginine + H2O
?
show the reaction diagram
substrate for isoform PAD4 only
-
-
?
CXC chemokine ligand 10 L-Arg + H2O
CXC chemokine ligand 10 citrulline + NH3
show the reaction diagram
-
-
-
-
?
CXC chemokine ligand 11 L-arginine + H2O
CXC chemokine ligand 11 L-citrulline + NH3
show the reaction diagram
-
-
-
-
?
CXCL17 L-Arg + H2O
CXCL17 L-citrulline + NH3
show the reaction diagram
-
-
-
?
CXCL26 L-Arg + H2O
CXCL26 L-citrulline + NH3
show the reaction diagram
-
-
-
?
CXCL5 L-Arg + H2O
CXCL5 L-citrulline + NH3
show the reaction diagram
-
-
-
?
CXCL8 L-Arg + H2O
CXCL8 L-citrulline + NH3
show the reaction diagram
citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
-
-
?
DDYSSSRDGYGGS + H2O
?
show the reaction diagram
substrate for isoform PAD4
-
-
?
DGYGGSRDSYSSS + H2O
?
show the reaction diagram
substrate for isoform PAD4
-
-
?
DSEGTWRKGPEAD + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
DSHKFDRDFIYSD + H2O
DSHKFDCitDFIYSD + NH3
show the reaction diagram
DSHKHSREWLWSD + H2O
DSHKHSCitEWLWSD + NH3
show the reaction diagram
DSHKWHRDFFYSD + H2O
DSHKWHCitDFFYSD + NH3
show the reaction diagram
DSKFAFRGGIASD + H2O
DSKFAFCitGGIASD + NH3
show the reaction diagram
DSKFHFRYAVASD + H2O
DSKFHFCitYAVASD + NH3
show the reaction diagram
DSKFKFRYAYASD + H2O
DSKFKFCitYAYASD + NH3
show the reaction diagram
DSKHFHRDFIYSD + H2O
DSKHFHCitDFIYSD + NH3
show the reaction diagram
DSKHKSRDFVYSD + H2O
DSKHKSCitDFVYSD + NH3
show the reaction diagram
DSKHLSREWMWSD + H2O
DSKHLSCitEWMWSD + NH3
show the reaction diagram
DSKKFDRDHLYSD + H2O
DSKKFDCitDHLYSD + NH3
show the reaction diagram
DSKKFDRGHLYSD + H2O
DSKKFDCitGHLYSD + NH3
show the reaction diagram
DSKKFHRDFLYSD + H2O
DSKKFHCitDFLYSD + NH3
show the reaction diagram
DSKKFHRGFLYSD + H2O
DSKKFHCitGFLYSD + NH3
show the reaction diagram
DSKKFKRDFLFSD + H2O
DSKKFKCitDFLFSD + NH3
show the reaction diagram
DSKKHDRDHLWSD + H2O
DSKKHDCitDHLWSD + NH3
show the reaction diagram
DSKKHFRDKLYSD + H2O
DSKKHFCitDKLYSD + NH3
show the reaction diagram
DSKKHFRGKLYSD + H2O
DSKKHFCitGKLYSD + NH3
show the reaction diagram
DSKKKHREWVWSD + H2O
DSKKKHCitEWVWSD + NH3
show the reaction diagram
DSKKLHRDHMESD + H2O
DSKKLHCitDHMESD + NH3
show the reaction diagram
DSKKYDRDFLWSD + H2O
DSKKYDCitDFLWSD + NH3
show the reaction diagram
DSKKYDRGFLWSD + H2O
DSKKYDCitGFLWSD + NH3
show the reaction diagram
DSKWHHRDHLYSD + H2O
DSKWHHCitDHLYSD + NH3
show the reaction diagram
DSKWHHRGHLYSD + H2O
DSKWHHCitGHLYSD + NH3
show the reaction diagram
DSKWYHRNKFWSD + H2O
DSKWYHCitNKFWSD + NH3
show the reaction diagram
DSQFAFRGASASD + H2O
DSQFAFCitGASASD + NH3
show the reaction diagram
DSQWAFRHALFSD + H2O
DSQWAFCitHALFSD + NH3
show the reaction diagram
DSRFYWRGGGKSD + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
DSSEELRGGGKSD + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
DSYRSWRDGYYSD + H2O
?
show the reaction diagram
substrate for isoform PAD4
-
-
?
FFDSHKFDRDFIYSD + H2O
FFDSHKFDCitDFIYSD + NH3
show the reaction diagram
FFDSHKHSREWLWSD + H2O
FFDSHKHSCitEWLWSD + NH3
show the reaction diagram
FFDSHKKSREYVFSD + H2O
FFDSHKKSCitEYVFSD + NH3
show the reaction diagram
FFDSHKLHREWMWSD + H2O
FFDSHKLHCitEWMWSD + NH3
show the reaction diagram
FFDSHKWHRDFFYSD + H2O
FFDSHKWHCitDFFYSD + NH3
show the reaction diagram
FFDSKHFDREWIWSD + H2O
FFDSKHFDCitEWIWSD + NH3
show the reaction diagram
FFDSKHKSRDFVYSD + H2O
FFDSKHKSCitDFVYSD + NH3
show the reaction diagram
FFDSKHLSREWMWSD + H2O
FFDSKHLSCitEWMWSD + NH3
show the reaction diagram
FFDSKKFSRDHIESD + H2O
FFDSKKFSCitDHIESD + NH3
show the reaction diagram
FFDSKKKHREWVWSD + H2O
FFDSKKKHCitEWVWSD + NH3
show the reaction diagram
FFDSKKWSREYFFSD + H2O
FFDSKKWSCitEYFFSD + NH3
show the reaction diagram
fibrin L-arginine + H2O
fibrin L-citrulline + NH3
show the reaction diagram
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrinogen with citrullinated L-arginine residues
show the reaction diagram
-
-
-
-
?
fibrinogen-L-arginine + H2O
fibrinogen-L-citrulline + NH3
show the reaction diagram
filaggrin + H2O
?
show the reaction diagram
filaggrin L-Arg + H2O
filaggrin citrulline + NH3
show the reaction diagram
-
-
-
?
filaggrin L-Arg + H2O
filaggrin L-citrulline + NH3
show the reaction diagram
-
-
-
-
?
filaggrin L-arginine + H2O
filaggrin L-citrulline + NH3
show the reaction diagram
filaggrin-L-arginine + H2O
filaggrin-L-citrulline + NH3
show the reaction diagram
gamma-actin L-arginine + H2O
gamma-actin L-citrulline + NH3
show the reaction diagram
substrate for isoform PAD2 only
-
-
?
glial fibrillary acidic protein L-arginine + H2O
glial fibrillary acidic protein L-citrulline + NH3
show the reaction diagram
-
-
-
?
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
show the reaction diagram
GYGGGSRDGSYGG + H2O
?
show the reaction diagram
substrate for isoform PAD4
-
-
?
histone H2A L-arginine + H2O
histone H2A L-citrulline + NH3
show the reaction diagram
-
deimination occurs at Arg3 of the N-terminal sequence acetyl-SGRGK
-
-
?
histone H2A-L-arginine + H2O
histone H2A-L-citrulline + NH3
show the reaction diagram
histone H3 L-arginine + H2O
histone H3 L-citrulline + NH3
show the reaction diagram
-
-
-
-
?
histone H3-L-Arg + H2O
histone H3-L-citrulline
show the reaction diagram
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
show the reaction diagram
histone H4 L-arginine + H2O
histone H4 L-citrulline + NH3
show the reaction diagram
-
deimination occurs at Arg3 of the N-terminal sequence acetyl-SGRGK
-
-
?
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
show the reaction diagram
histone L-arginine + H2O
histone L-citrulline + NH3
show the reaction diagram
IEIITDRQSGKKR + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
IEIMTDRGSGKKR + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
IGSRGDRSGFGKF + H2O
?
show the reaction diagram
substrate for isoform PAD2
-
-
?
KDRNW + H2O
?
show the reaction diagram
-
-
-
-
?
keratin L-arginine + H2O
keratin L-citrulline + NH3
show the reaction diagram
keratin-L-arginine + H2O
keratin-L-citrulline + NH3
show the reaction diagram
KKSIRDTPA + H2O
KKSI-citrulline-DTPA
show the reaction diagram
-
-
-
?
KSIRDTP + H2O
KSI-citrulline-DTP
show the reaction diagram
-
-
-
?
LDRGE + H2O
?
show the reaction diagram
-
-
-
-
?
MWRHV + H2O
?
show the reaction diagram
-
-
-
-
?
myelin basic protein L-arginine + H2O
myelin basic protein L-citrulline + NH3
show the reaction diagram
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
show the reaction diagram
N-alpha-benzoyl-L-arginine amide + H2O
N-alpha-benzoyl-L-citrulline amide + NH3
show the reaction diagram
-
best small molecule substrate for isozyme PAD1
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline methyl ester + NH3
show the reaction diagram
-
-
-
?
N-alpha-benzoyl-L-arginine methyl ester + H2O
N-alpha-benzoyl-L-citrulline methyl ester + NH3
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl L-arginine ethyl ester + H2O
Nalpha-benzoyl L-citrulline ethyl ester + NH3
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
Nalpha-benzoyl-L-citrulline + NH3
show the reaction diagram
Nalpha-benzoyl-L-arginine amide + H2O
Nalpha-benzoyl-L-citrulline amide + NH3
show the reaction diagram
Nalpha-benzoyl-L-arginine ethyl ester
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
Nalpha-benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
Nalpha-benzoyl-L-arginine methyl ester + H2O
Nalpha-benzoyl-L-citrulline methyl ester + NH3
show the reaction diagram
p300-L-arginine + H2O
?
show the reaction diagram
-
-
-
-
?
PAD4-L-arginine + H2O
PAD4-L-citrulline + NH3
show the reaction diagram
-
PAD4 is autodeiminated in a time-dependent manner
-
-
?
peptide H3-1-L-arginine + H2O
peptide H3-1-L-citrulline + NH3
show the reaction diagram
i.e. Ac4KQTARKSTGG13
-
-
?
peptide H3-2-L-arginine + H2O
peptide H3-2-L-citrulline + NH3
show the reaction diagram
i.e. Ac14KAPRKQLATK23
-
-
?
peptide H4-L-arginine + H2O
peptide H4-L-citrulline + NH3
show the reaction diagram
-
i.e. Ac1SGRGKGGKGL10
-
?
protein L-Arg + H2O
protein citrulline + NH3
show the reaction diagram
-
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
show the reaction diagram
protein-L-arginine + H2O
protein-L-citrulline + NH3
show the reaction diagram
QLSLRTVSL + H2O
QLSL-citrulline-TVSL
show the reaction diagram
-
-
-
?
S100A3-L-arginine + H2O
S100A3-L-citrulline + NH3
show the reaction diagram
-
-
-
?
SHQESTRGKSKGKAAAAA + H2O
SHQEST-Cit-GKSKGKAAAAA + NH3
show the reaction diagram
-
-
-
?
SIRDT + H2O
SI-citrulline-RDT
show the reaction diagram
-
-
-
?
TKQTARKSTGGK + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Arg-ethyl ester + H2O
tosyl-citrulline-ethyl ester + NH3
show the reaction diagram
-
hPADI2
-
-
?
TSTGGRQGSHH + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin-L-arginine + H2O
vimentin-L-citrulline + NH3
show the reaction diagram
vimetin L-arginine + H2O
vimentin L-citrulline + NH3
show the reaction diagram
WSRYH + H2O
?
show the reaction diagram
-
-
-
-
?
WTRGE + H2O
?
show the reaction diagram
-
-
-
-
?
YWRDH + H2O
?
show the reaction diagram
-
-
-
-
?
[histone H4]-L-Arg + H2O
[histone H4]-L-citrulline + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protein L-arginine + H2O
protein L-citrulline + NH3
show the reaction diagram
trichohyalin-L-arginine + H2O
trichohyalin-L-citrulline + NH3
show the reaction diagram
PAD3, involvement in skin disease
-
-
ir
fibrin L-arginine + H2O
fibrin L-citrulline + NH3
show the reaction diagram
-
citrullinated fibrin is a potential antigen of rheumatoid arthritis
-
-
?
fibrinogen-L-arginine + H2O
fibrinogen-L-citrulline + NH3
show the reaction diagram
PAD4, involvement in rheumatoid arthritis
-
-
ir
filaggrin-L-arginine + H2O
filaggrin-L-citrulline + NH3
show the reaction diagram
PAD4, involvement in rheumatoid arthritis
-
-
ir
glial fibrillary acidic protein L-arginine + H2O
glial fibrillary acidic protein L-citrulline + NH3
show the reaction diagram
-
-
-
?
glial fibrillary acidic protein-L-arginine + H2O
glial fibrillary acidic protein-L-citrulline + NH3
show the reaction diagram
PAD2, involvement in Alzheimer's diease
-
-
ir
histone H2A-L-arginine + H2O
histone H2A-L-citrulline + NH3
show the reaction diagram
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone H3-L-Arg + H2O
histone H3-L-citrulline
show the reaction diagram
-
PADI4 is a histone H3-specific arginine deiminase. Deimination is a mechanism for antagonizing the transcriptional induction mediated by arginine methylation
-
-
?
histone H3-L-arginine + H2O
histone H3-L-citrulline + NH3
show the reaction diagram
histone H4-L-arginine + H2O
histone H4-L-citrulline + NH3
show the reaction diagram
PAD4, involvement in rheumatoid arthritis
-
-
ir
histone L-arginine + H2O
histone L-citrulline + NH3
show the reaction diagram
-
PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones
-
-
?
keratin-L-arginine + H2O
keratin-L-citrulline + NH3
show the reaction diagram
myelin basic protein-L-arginine + H2O
myelin basic protein-L-citrulline + NH3
show the reaction diagram
protein L-Arg + H2O
protein citrulline + NH3
show the reaction diagram
-
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
protein L-arginine + H2O
protein L-citrulline + NH3
show the reaction diagram
protein-L-arginine + H2O
protein-L-citrulline + NH3
show the reaction diagram
vimentin-L-arginine + H2O
vimentin-L-citrulline + NH3
show the reaction diagram
PAD2, involvement in Alzheimer's disease
-
-
ir
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
Ba2+ activates isozymes PAD 1 and 3 to about 15% and 2.5%, respectively, of the level of Ca2+
additional information
-
little to no activity is observed with Mg2+, Mn2+, Zn2+ even after long incubation times (up to 2 h)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
-
2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
-
2-chloro-N-[3-(2,5-dioxo-1-phenylimidazolidin-4-yl)propyl]ethanimidamide
-
2-chloro-N-[3-(2,5-dioxoimidazolidin-4-yl)propyl]ethanimidamide
-
2-{[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]carbamoyl}benzoic acid
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
4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-2-ethoxy-N-(4-methoxyphenyl)benzamide
-
4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-2-methoxy-N-(4-methoxyphenyl)benzamide
-
4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-N-(4-methoxyphenyl)benzamide
-
4-(4-{3-[(2-chloroethanimidoyl)amino]propyl}-2,5-dioxoimidazolidin-1-yl)-N-phenylbenzamide
-
4-chloromercuribenzoate
inhibits PAD3
4-[(2-chloroethanimidoyl)amino]-N-(diphenylmethyl)butanamide
-
chloro-N-(3-{1-[(2'-chloro-3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
-
chloro-N-(3-{1-[(2'-chloro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
-
chloro-N-(3-{1-[(3'-fluoro[1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)ethanimidamide
-
chloroamidine
iodoacetate
inhibits PAD3
N-(3-{1-[([1,1'-biphenyl]-3-yl)methyl]-2,5-dioxoimidazolidin-4-yl}propyl)(chloro)ethanimidamide
-
N-(biphenyl-3-ylmethyl)-4-[(2-chloroethanimidoyl)amino]butanamide
-
N-[(1R)-1-(biphenyl-3-yl)ethyl]-4-[(2-chloroethanimidoyl)amino]butanamide
-
N-[(1S)-1-(biphenyl-3-yl)ethyl]-4-[(2-chloroethanimidoyl)amino]butanamide
-
N-[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
-
N-[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
-
N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
-
N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
-
N-[(3'-bromobiphenyl-3-yl)methyl]-4-[(2-chloroethanimidoyl)amino]butanamide
-
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-[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
-
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}[1,1'-biphenyl]-4-carboxamide
-
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}benzamide
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
(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-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-chloroethaniminium
-
-
1-[[4-(benzoylamino)-5-(ethylamino)-5-oxopentyl]amino]-2-fluoroethaniminium
-
-
1-[[6-amino-5-(benzoylamino)-6-oxohexyl]amino]-2-chloroethaniminium
-
potent, irreversible and specific PAD3 inhibitor
1-[[6-amino-5-(benzoylamino)-6-oxohexyl]amino]-2-fluoroethaniminium
-
potent, irreversible and specific PAD3 inhibitor
2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
-
2-({(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}carbamoyl)benzoic acid
-
2-chloroacetamidine
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
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
5-aminosalicylic acid
-
-
Azathioprine
-
-
azithromycin
-
-
BAPTA-AM
inhibits PAD2
benzoyl-N-dimethyl-Arg
inhibits PAD4
benzoyl-N-methyl-Arg
inhibits PAD4
benzoyl-Ngamma,Ngamma-dimethyl-Arg
IC50: 0.4 mM
benzoyl-Ngamma-methyl-Arg
-
chloroamidine
chlortetracycline
-
-
Cl-amidine
clindamycin
-
-
F-amidine
interferon beta
inhibits PAD2
-
iodoacetamide
-
-
leflunomide
-
-
methotrexate
-
-
minocycline
-
a mixed type inhibitor
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine ethyl ester
complete inhibition of recombinant PAD4 at 2 mM
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-[(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)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
-
N-[(1S)-4-[(2-chloroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
-
N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl]benzamide
-
N-[(1S)-4-[(2-fluoroethanimidoyl)amino]-1-(2H-tetrazol-5-yl)butyl][1,1'-biphenyl]-4-carboxamide
-
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-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}benzamide
-
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-chloroethanimidoyl)amino]butyl}[1,1'-biphenyl]-4-carboxamide
-
N-{(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl}benzamide
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
N-{(2S)-1-amino-5-[(2-chloroethanimidoyl)amino]-1-oxopentan-2-yl}benzamide
-
-
N-{(2S)-1-amino-5-[(2-fluoroethanimidoyl)amino]-1-oxopentan-2-yl}benzamide
-
-
N2-benzoyl-N5-(N,N-dimethylcarbamimidoyl)-L-ornithine
-
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
paclitaxel
streptomycin
-
a competitive inhibitor of PAD4
sulfamethoxazole
-
-
sulfapyridine
-
-
tetracycline
-
-
trimethoprim
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
66.3
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
33.6
benzoyl-L-Arg
pH 7.6, 55°C, peptidylarginine deiminase 3
7.5
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
0.11 - 0.18
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
0.32 - 0.36
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
0.3 - 0.95
Ac-Ala-Gly-Arg-Gly-Lys
0.69 - 0.8
Ac-Ser-Ala-Arg-Gly-Lys
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
0.16 - 0.58
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
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
0.15 - 0.59
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
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
0.22 - 1.95
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
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
0.91
acetyl-L-Arg
pH 7.6, 55°C, peptidylarginine deiminase 1
1.19 - 3.73
acetyl-L-Arg methyl ester
0.15 - 0.91
benzoyl-Arg-ethyl ester
0.63 - 1.97
benzoyl-Arg-methyl ester
0.16 - 1.23
benzoyl-Arg-NH2
0.38 - 1.49
benzoyl-L-Arg
0.35 - 0.5
benzoyl-L-Arg ethyl ester
0.41
benzoyl-L-arginine
37°C
0.25
benzoyl-L-arginine amide
37°C
1.36
benzoyl-L-arginine ethyl ester
37°C
1.66
benzoyl-L-arginine methyl ester
37°C
0.013 - 0.055
fibrinogen
-
0.001 - 0.064
filaggrin
-
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
0.325
KDRNW
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.45
LDRGE
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.27
MWRHV
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.16 - 17.5
N-alpha-benzoyl-L-arginine amide
0.1 - 30
N-alpha-benzoyl-L-arginine ethyl ester
0.37 - 10.8
N-alpha-benzoyl-L-arginine methyl ester
0.44 - 1.7
Nalpha-benzoyl L-arginine ethyl ester
0.41 - 1.6
Nalpha-benzoyl-L-arginine
0.25 - 0.48
Nalpha-benzoyl-L-arginine amide
0.27 - 2.77
Nalpha-benzoyl-L-arginine ethyl ester
0.24 - 1.66
Nalpha-benzoyl-L-arginine methyl ester
0.372
TKQTARKSTGGK
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
1.63 - 5.61
tosyl-Arg-ethyl ester
0.575
TSTGGRQGSHH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.12
WSRYH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.345
WTRGE
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.187
YWRDH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.088 - 0.35
[histone H4]-L-Arg
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.93
acetyl-L-Arg methyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
0.79
benzoyl-L-Arg
pH 7.6, 55°C, peptidylarginine deiminase 3
1.73
benzoyl-L-Arg ethyl ester
pH 7.6, 55°C, peptidylarginine deiminase 3
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
0.21 - 0.59
Ac-Ala-Gly-Arg-Gly-Lys
0.62 - 1.13
Ac-Ser-Ala-Arg-Gly-Lys
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
0.75 - 2.53
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
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
0.08 - 2.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
0.64 - 4.92
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
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
13.68
acetyl-L-Arg
pH 7.6, 55°C, peptidylarginine deiminase 1
0.057 - 11.28
acetyl-L-Arg methyl ester
0.52 - 14.43
benzoyl-L-Arg
0.057 - 15.24
benzoyl-L-Arg ethyl ester
3.35
benzoyl-L-arginine
37°C
2.76 - 6
benzoyl-L-arginine amide
5.94
benzoyl-L-arginine ethyl ester
37°C
5.57
benzoyl-L-arginine methyl ester
37°C
2
KDRNW
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
2.9
LDRGE
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
2
MWRHV
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
1.85 - 3.57
N-alpha-benzoyl-L-arginine amide
0.03 - 11.7
N-alpha-benzoyl-L-arginine ethyl ester
1.26 - 5.57
N-alpha-benzoyl-L-arginine methyl ester
0.55 - 3.8
Nalpha-benzoyl L-arginine ethyl ester
0.63
Nalpha-benzoyl-L-arginine
at pH 7.6 and 37°C
0.32
Nalpha-benzoyl-L-arginine amide
at pH 7.6 and 37°C
3.2 - 13.9
Nalpha-benzoyl-L-arginine ethyl ester
0.43
Nalpha-benzoyl-L-arginine methyl ester
at pH 7.6 and 37°C
0.7
TKQTARKSTGGK
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
1.3
TSTGGRQGSHH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
1.8
WSRYH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
3.3
WTRGE
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
2.3
YWRDH
-
in 60 mM MOPS buffer, pH 7.5 and 10 mM CaCl2, at 37°C
0.49 - 2.1
[histone H4]-L-Arg
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 5.7
2-acetyl-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
0.001 - 1.4
3-acetyl-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
0.22 - 3.5
Ac-Ala-Gly-Arg-Gly-Lys
0.9 - 5.8
Ac-Ser-Ala-Arg-Gly-Lys
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
0.08 - 6.6
Ac-Ser-Gly-Arg-Ala-Lys
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
0.05 - 16
Ac-Ser-Gly-Arg-Gly-Ala
0.001 - 3.3
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly
2 - 4.6
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala
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
0.5 - 3.9
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys
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
2.5 - 4.4
Ac-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His
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
0.7 - 9
histone H4-L-arginine
0.13 - 120000
N-alpha-benzoyl-L-arginine amide
0.005 - 13800
N-alpha-benzoyl-L-arginine ethyl ester
0.12 - 10.4
N-alpha-benzoyl-L-arginine methyl ester
0.63 - 6.4
Nalpha-benzoyl L-arginine ethyl ester
0.39
Nalpha-benzoyl-L-arginine
at pH 7.6 and 37°C
0.68
Nalpha-benzoyl-L-arginine amide
at pH 7.6 and 37°C
11.7
Nalpha-benzoyl-L-arginine ethyl ester
at pH 7.6 and 37°C
1.8
Nalpha-benzoyl-L-arginine methyl ester
at pH 7.6 and 37°C
0.0031 - 10
[histone H4]-L-Arg
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0059
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide
-
0.0216
N-alpha-benzoyl-N5-(2-fluoro-1-iminoethyl)-L-ornithine amide
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0028 - 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
10
5-aminosalicylic acid
Homo sapiens
-
above, pH 7.6, 37°C, recombinant PAD4
8.1
Azathioprine
Homo sapiens
-
pH 7.6, 37°C, recombinant PAD4
10
azithromycin
Homo sapiens
-
above, pH 7.6, 37°C, recombinant PAD4
0.4
benzoyl-Ngamma,Ngamma-dimethyl-Arg
Homo sapiens
IC50: 0.4 mM
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
0.0008 - 0.022
Cl-amidine
5.1
clindamycin
Homo sapiens
-
pH 7.6, 37°C, recombinant PAD4
0.0216 - 0.35
F-amidine
0.13
H2O2
Homo sapiens
pH 7.4, 23°C
2.4
leflunomide
Homo sapiens
-
pH 7.6, 37°C, recombinant PAD4
10
methotrexate
Homo sapiens
-
above, pH 7.6, 37°C, recombinant PAD4
0.5
N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine ethyl ester
Homo sapiens
recombinant PAD4, pH 7.6, 37°C
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)
1.8
streptomycin
Homo sapiens
-
pH 7.6, 37°C, recombinant PAD4
10
sulfamethoxazole
Homo sapiens
-
above, pH 7.6, 37°C, recombinant PAD4
10
sulfapyridine
Homo sapiens
-
above, pH 7.6, 37°C, recombinant PAD4
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
7.5
trimethoprim
Homo sapiens
-
pH 7.6, 37°C, recombinant PAD4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
deamination of fillagrin, peptidylarginine deiminase 3
7
-
hPADI2
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform PAD3 is expressed in granular level of stratum corneum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
thyroid, moderate expression
Manually annotated by BRENDA team
brain, moderate expression
Manually annotated by BRENDA team
-
PADI4 is significantly overexpressed in blood of rheumatoid arthritis. Genetic variation within PADI4 is not a major risk factor for rheumatoid arzhritis in Caucasians
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
high amount of PAD2
Manually annotated by BRENDA team
low expression level of PAD1
Manually annotated by BRENDA team
strong expression
Manually annotated by BRENDA team
-
abnormal accumulation of citrullinated proteins and abnormal activation of PAD2 in hippocampi of patients with Alzheimer's disease
Manually annotated by BRENDA team
-
T-cell leukemia cell line with tetracycline resistance
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
-
in adult mainly expressed in ovary and peripheral blood leukocytes
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
quantitative determination of PAD2 and PAD4 by immunohistochemistry
Manually annotated by BRENDA team
fetal, increased amounts of PAD3
Manually annotated by BRENDA team
strong expression
Manually annotated by BRENDA team
-
in adult mainly expressed in ovary and peripheral blood leukocytes
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
expression of isoform PAD2
Manually annotated by BRENDA team
-
high abundance of PADI14 in the synovial membrane is a prominent feature of rheumatoid arthritis
Manually annotated by BRENDA team
-
slight expression
Manually annotated by BRENDA team
moderate expression
Manually annotated by BRENDA team
-
slight expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
calcium-dependent histone-modifying enzymes whose activity is dysregulated in inflammatory diseases and cancer
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PADI3_HUMAN
664
0
74743
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76000
x * 76000, His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 76000, His-tagged enzyme, SDS-PAGE
dimer
-
dimerization of PAD4 is essential for full enzyme activity and calcium-binding cooperativity
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
methylation of Arg107 is a naturally occuring modification of the enzyme that affects deimination of Arg residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20 mM imidazole buffer pH 7.0, 0.2 M Li2SO4, 15% (w/v) polyethylene glycol monomethylether 5000
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
Ca2+-free 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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A112G
-
K0.5 for Ca2+ higher than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
A82V
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
A82V/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
C434A
small decrase in kcat/Km value
C645A
C647A
loss of activity
D123N
D125A
D166A
D169A
D177A
D273A/R544A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.35 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.5/sec, quaternary structure: dimer, Kd: 0.68 microM
D350A
no enzymic activity, catalytic residue
D369A
no enzymic activity, ligand for Ca2 coordination
D370A
D374A
D388A
81% of wild type activity, ligand for Ca4 coordination
D389A
D465A
residue involved in dimerization, about 30% of wild-type catalytic effciency
D473A
no enzymic activity, catalytic residue
D547A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 11.6/sec, quaternary structure: monomer/dimer, Kd: 6.4 microM
D547E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.72 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 8.9/sec, quaternary structure: monomer/dimer, Kd: 11.2 microM
D547N
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.86 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 4.9 microM
E281A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.45 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.1/sec, quaternary structure: dimer, Kd: 0.1 microM
E351A
33% of wild type activity, ligand for Ca2 coordination
E352A
E353A
no enzymic activity, ligand for Ca1 coordination
E354A
2000fold decrease in activity
E411A
no enzymic activity, ligand for Ca1 coordination
E412A
F221A/F222A
F285AV284A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
F541A
residue at dimer interface, about 50% decrease in kcat/Km value
F576A
residue at dimer interface, about 50% decrease in kcat/Km value
G374R
-
the PAD3 mutant does not display PAD4-like kinetics with benzoylated arginine derivatives
H471A
no enzymic activity, catalytic residue
L279A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L279D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L279I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
L6I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
N373A
no enzymic activity, ligand for Ca2 coordination
N648A
37% of wild type activity, ligand for water-mediated Ca1 coordination
Q349A
no enzymic activity, ligand for Ca1 coordination
Q350A
R123K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R123Q
-
K0.5 for Ca2+ higher than that obtained with the R123K mutant, but lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R156K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R156Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R205K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R205Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R347A
R372A
almost complete loss of activity
R372K
R372Q
R373A
2000fold decrease in activity
R374K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R374Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R419K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) comparable to wild-type
R419Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R441A
residue involved in dimerization, about 6% of wild-type catalytic effciency
R484K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R484Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R609K
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R609Q
-
K0.5 for Ca2+ comparable to wild-type, kcat/Km ([histone H4]-L-Arg) lcomparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R639A
about 30% decrease in kcat/Km value
R639K
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R639Q
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) comparable to wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) lower than wild-type
R8A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.47 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 9.3 microM
R8A/D547A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.4 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 10.7/sec, quaternary structure: monomer/dimer, Kd: 3.9 microM
R8E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 1.06 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 7.3/sec, quaternary structure: monomer, Kd: 45.6 microM
R8E/D547E
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 2.77 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 3.3/sec, quaternary structure: monomer, Kd: 24 microM
R8H
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.47 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.3/sec, quaternary structure: dimer, Kd: 0.47 microM
R8K
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.5 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 10.8/sec, quaternary structure: monomer/dimer, Kd: 10.2 microM
R8L
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 1.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 5.3/sec, quaternary structure: monomer, Kd: 16.8 microM
R8Q
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.6 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 12.2/sec, quaternary structure: monomer/dimer, Kd: 15.7 microM
S55G
-
K0.5 for Ca2+ lower than wild-type, kcat/Km ([histone H4]-L-Arg) lower than wild-type, kcat/Km (Nalpha-benzoyl L-arginine ethyl ester) higher than wild-type
S55G/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
S55G/A82V
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows reduced activity compared to the wild-type PADI4
S55G/A82V/A112G
-
naturally occuring single-nucleotide polymorphisms and site-directed mutagenesis, the SNP-PADI4 mutant haplotype shows a higher risk of rheumatoid arthritis due to correlation with the RA gene, because the mutant shows increased activity, compared to the wild-type PADI4, which promotes the autoimmune disease and apoptosis, overview
V283A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V283T
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284A
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284D
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V284I
residue at dimer interface. Mutation decreases dimer formation and, consequently, enzyme activity
V469A
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
V469L
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
V469T
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W347A
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W347F
residue is critical for substrate binding at the active site. Mutation leads to a severe reduction in the catalytic activity
W348A
loss of activity
W373A
50fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
W548A
residue at dimer interface, complete loss of activity
W548F
residue at dimer interface, about 50% decrease in kcat/Km value
W548K
residue at dimer interface, about 50% decrease in kcat/Km value
Y237A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.36 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.9/sec, quaternary structure: dimer, Kd: 0.29 microM
Y237A/E281A
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 0.38 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 13.2/sec, quaternary structure: dimer, Kd: 0.1 microM
Y435A
Y435N
-
Km (Nalpha-benzoyl-L-arginine ethyl ester): 2.73 mM, kcat (Nalpha-benzoyl-L-arginine ethyl ester): 4/sec, quaternary structure: monomer, Kd: 33.8 microM
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
melting temperature, mutants L6D, L6I
46
melting temperature, mutant D465A
51
melting temperature, wild-type
55
melting temperature, mutant V283T
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag affinity column chromatography and Sephacryl S-200 gel filtration
glutathione-Sepharose 4B column chromatography
-
Ni-NTA-agarose resin, column chromatography, and gel filtration
Ni2+-charged HiTrap column chromatography and Sephacryl S-200 gel filtration
Ni2+-NTA-agarose column chromatography
recombinant
recombinant GST-tagged PAD4 mutant C645A by glutathione affinity chromatography
recombinant Pad4
recombinant peptidylarginine deiminase 1
recombinant peptidylarginine deiminase 2
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
expressed in Mus musculus
expression analysis
expression in Escherichia coli
expression of PAD4
gene padi4, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
-
hPADI2 is expressed in Escherichia coli
-
hPADI4 is expressed in Escherichia coli
-
overexpression in Escherichia coli
overexpression of GST-tagged PAD4 mutant C645A
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
camptothecin and staurosporine fail to stimulate PAD activity in HL-60 cells
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
PAD3 is a target in skin diseases including psoriasis, PAD3-like protein is a target for treatment of certain cancers
analysis
drug development
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pritzker, L.B.; Joshi, S.; Harauz, G.; Moscarello, M.A.
Deimination of myelin basic protein 3.5.3.15. Effect of methylation of MBP on its deimination by peptidylarginine deiminase
Biochemistry
39
5382-5388
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Arita, K.; Hashimoto, H.; Shimizu, T.; Yamada, M.; Sato, M.
Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase V
Acta Crystallogr. Sect. D
59
2332-2333
2003
Homo sapiens
Manually annotated by BRENDA team
Arita, K.; Hashimoto, H.; Shimizu, T.; Nakashima, K.; Yamada, M.; Sato, M.
Structural basis for Ca2+-induced activation of human PAD4
Nat. Struct. Mol. Biol.
11
777-783
2004
Homo sapiens (Q9UM07), Homo sapiens
Manually annotated by BRENDA team
Zhang, J.; Dai, J.; Zhao, E.; Lin, Y.; Zeng, L.; Chen, J.; Zheng, H.; Wang, Y.; Li, X.; Ying, K.; Xie, Y.; Mao, Y.
cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI
Acta Biochim. Pol.
51
1051-1058
2004
Homo sapiens
Manually annotated by BRENDA team
Vossenaar, E.R.; Radstake, T.R.; van der Heijden, A.; van Mansum, M.A.; Dieteren, C.; de Rooij, D.J.; Barrera, P.; Zendman, A.J.; van Venrooij, W.J.
Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages
Ann. Rheum. Dis.
63
373-381
2004
Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Sambandam, T.; Belousova, M.; Accaviti-Loper, M.A.; Blanquicett, C.; Guercello, V.; Raijmakers, R.; Nicholas, A.P.
Increased peptidylarginine deiminase type II in hypoxic astrocytes
Biochem. Biophys. Res. Commun.
325
1324-1329
2004
Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Nakayama-Hamada, M.; Suzuki, A.; Kubota, K.; Takazawa, T.; Ohsaka, M.; Kawaida, R.; Ono, M.; Kasuya, A.; Furukawa, H.; Yamada, R.; Yamamoto, K.
Comparison of enzymatic properties between hPADI2 and hPADI4
Biochem. Biophys. Res. Commun.
327
192-200
2005
Homo sapiens
Manually annotated by BRENDA team
Dong, S.; Kanno, T.; Yamaki, A.; Kojima, T.; Shiraiwa, M.; Kawada, A.; Mechin, M.C.; Chavanas, S.; Serre, G.; Simon, M.; Takahara, H.
NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes
Biochem. J.
397
449-459
2006
Homo sapiens (Q9ULW8), Homo sapiens
Manually annotated by BRENDA team
Kearney, P.L.; Bhatia, M.; Jones, N.G.; Yuan, L.; Glascock, M.C.; Catchings, K.L.; Yamada, M.; Thompson, P.R.
Kinetic characterization of protein arginine deiminase 4: a transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis
Biochemistry
44
10570-10582
2005
Homo sapiens (Q9UM07), Homo sapiens
Manually annotated by BRENDA team
Stone, E.M.; Schaller, T.H.; Bianchi, H.; Person, M.D.; Fast, W.
Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: dimethylargininase and peptidylarginine deiminase
Biochemistry
44
13744-13752
2005
Homo sapiens (Q9UM07), Homo sapiens
Manually annotated by BRENDA team
Hagiwara, T.; Hidaka, Y.; Yamada, M.
Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes
Biochemistry
44
5827-5834
2005
Homo sapiens
Manually annotated by BRENDA team
Cuthbert, G.L.; Daujat, S.; Snowden, A.W.; Erdjument-Bromage, H.; Hagiwara, T.; Yamada, M.; Schneider, R.; Gregory, P.D.; Tempst, P.; Bannister, A.J.; Kouzarides, T.
Histone deimination antagonizes arginine methylation
Cell
118
545-553
2004
Homo sapiens
Manually annotated by BRENDA team
Mechin, M.C.; Enji, M.; Nachat, R.; Chavanas, S.; Charveron, M.; Ishida-Yamamoto, A.; Serre, G.; Takahara, H.; Simon, M.
The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations
Cell. Mol. Life Sci.
62
1984-1995
2005
Homo sapiens, Homo sapiens (Q9ULC6), Homo sapiens (Q9ULW8)
Manually annotated by BRENDA team
Hidaka, Y.; Hagiwara, T.; Yamada, M.
Methylation of the guanidino group of arginine residues prevents citrullination by peptidylarginine deiminase IV
FEBS Lett.
579
4088-4092
2005
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Nachat, R.; Mechin, M.C.; Takahara, H.; Chavanas, S.; Charveron, M.; Serre, G.; Simon, M.
Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin
J. Invest. Dermatol.
124
384-393
2005
Homo sapiens (Q9ULC6), Homo sapiens (Q9ULW8), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Nachat, R.; Mechin, M.C.; Charveron, M.; Serre, G.; Constans, J.; Simon, M.
Peptidylarginine deiminase isoforms are differentially expressed in the anagen hair follicles and other human skin appendages
J. Invest. Dermatol.
125
34-41
2005
Homo sapiens, Homo sapiens (Q9ULW8), Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Ishigami, A.; Ohsawa, T.; Hiratsuka, M.; Taguchi, H.; Kobayashi, S.; Saito, Y.; Murayama, S.; Asaga, H.; Toda, T.; Kimura, N.; Maruyama, N.
Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease
J. Neurosci. Res.
80
120-128
2005
Homo sapiens
Manually annotated by BRENDA team
Chang, X.; Han, J.
Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors
Mol. Carcinog.
45
183-196
2006
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Arita, K.; Shimizu, T.; Hashimoto, H.; Hidaka, Y.; Yamada, M.; Sato, M.
Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4
Proc. Natl. Acad. Sci. USA
103
5291-5296
2006
Homo sapiens, Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Kubota, K.; Yoneyama-Takazawa, T.; Ichikawa, K.
Determination of sites citrullinated by peptidylarginine deiminase using 18O stable isotope labeling and mass spectrometry
Rapid Commun. Mass Spectrom.
19
683-688
2005
Homo sapiens
Manually annotated by BRENDA team
Chang, X.; Yamada, R.; Suzuki, A.; Sawada, T.; Yoshino, S.; Tokuhiro, S.; Yamamoto, K.
Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis
Rheumatology
44
40-50
2005
Homo sapiens
Manually annotated by BRENDA team
Harney, S.M.; Meisel, C.; Sims, A.M.; Woon, P.Y.; Wordsworth, B.P.; Brown, M.A.
Genetic and genomic studies of PADI4 in rheumatoid arthritis
Rheumatology
44
869-872
2005
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Wysocka, J.; Sayegh, J.; Lee, Y.H.; Perlin, J.R.; Leonelli, L.; Sonbuchner, L.S.; McDonald, C.H.; Cook, R.G.; Dou, Y.; Roeder, R.G.; Clarke, S.; Stallcup, M.R.; Allis, C.D.; Coonrod, S.A.
Human PAD4 regulates histone arginine methylation levels via demethylimination
Science
306
279-283
2004
Homo sapiens
Manually annotated by BRENDA team
Zendman, A.J.; Raijmakers, R.; Nijenhuis, S.; Vossenaar, E.R.; Tillaart, M.; Chirivi, R.G.; Raats, J.M.; van Venrooij, W.J.; Drijfhout, J.W.; Pruijn, G.J.
ABAP: antibody-based assay for peptidylarginine deiminase activity
Anal. Biochem.
369
232-240
2007
Oryctolagus cuniculus, Mus musculus, Homo sapiens (Q9Y2J8), Homo sapiens, Mus musculus C57BL/6 / 129S
Manually annotated by BRENDA team
Hung, H.C.; Lin, C.Y.; Liao, Y.F.; Hsu, P.C.; Tsay, G.J.; Liu, G.Y.
The functional haplotype of peptidylarginine deiminase IV (S55G, A82V and A112G) associated with susceptibility to rheumatoid arthritis dominates apoptosis of acute T leukemia Jurkat cells
Apoptosis
12
475-487
2007
Homo sapiens
Manually annotated by BRENDA team
Luo, Y.; Arita, K.; Bhatia, M.; Knuckley, B.; Lee, Y.H.; Stallcup, M.R.; Sato, M.; Thompson, P.R.
Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization
Biochemistry
45
11727-11736
2006
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Knuckley, B.; Luo, Y.; Thompson, P.R.
Profiling protein arginine deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors
Bioorg. Med. Chem.
16
739-745
2008
Homo sapiens
Manually annotated by BRENDA team
Keilhoff, G.; Prell, T.; Langnaese, K.; Mawrin, C.; Simon, M.; Fansa, H.; Nicholas, A.P.
Expression pattern of peptidylarginine deiminase in rat and human Schwann cells
Dev. Neurobiol.
68
101-114
2007
Homo sapiens, Homo sapiens (Q9ULC6), Homo sapiens (Q9Y2J8), Rattus norvegicus
Manually annotated by BRENDA team
Algeciras, M.E.; Bhattacharya, S.K.
Targeting optic nerve citrullination in glaucoma: a role for protein-arginine deiminase 2 (PAD2) inhibitors
Drugs Future
32
999-1005
2007
Homo sapiens, Homo sapiens (Q6TGC4), Homo sapiens (Q9ULC6), Homo sapiens (Q9ULW8), Homo sapiens (Q9Y2J8), Rattus norvegicus, Rattus norvegicus (O88806), Rattus norvegicus (O88807), Rattus norvegicus (P20717), Rattus norvegicus (P70708)
-
Manually annotated by BRENDA team
Dong, S.; Ying, S.; Kojima, T.; Shiraiwa, M.; Kawada, A.; Mechin, M.C.; Adoue, V.; Chavanas, S.; Serre, G.; Simon, M.; Takahara, H.
Crucial roles of MZF1 and Sp1 in the transcriptional regulation of the peptidylarginine deiminase type I gene (PADI1) in human keratinocytes
J. Invest. Dermatol.
128
549-557
2008
Homo sapiens (Q9ULC6), Homo sapiens
Manually annotated by BRENDA team
Wood, D.D.; Ackerley, C.A.; Brand, B.; Zhang, L.; Raijmakers, R.; Mastronardi, F.G.; Moscarello, M.A.
Myelin localization of peptidylarginine deiminases 2 and 4: comparison of PAD2 and PAD4 activities
Lab. Invest.
88
354-364
2008
Homo sapiens, Mus musculus (Q08642), Mus musculus (Q9Z183), Mus musculus CD-1 (Q08642), Mus musculus CD-1 (Q9Z183)
Manually annotated by BRENDA team
Makrygiannakis, D.; Hermansson, M.; Ulfgren, A.K.; Nicholas, A.P.; Zendman, A.J.; Eklund, A.; Grunewald, J.; Skold, C.M.; Klareskog, L.; Catrina, A.I.
Smoking increases peptidylarginine deiminase 2 enzyme expression in human lungs and increases citrullination in BAL cells
Ann. Rheum. Dis.
67
1488-1492
2008
Homo sapiens
Manually annotated by BRENDA team
Musse, A.A.; Polverini, E.; Raijmakers, R.; Harauz, G.
Kinetics of human peptidylarginine deiminase 2 (hPAD2)--reduction of Ca2+ dependence by phospholipids and assessment of proposed inhibition by paclitaxel side chains
Biochem. Cell Biol.
86
437-447
2008
Homo sapiens
Manually annotated by BRENDA team
Stensland, M.E.; Pollmann, S.; Molberg, ?.; Sollid, L.M.; Fleckenstein, B.
Primary sequence, together with other factors, influence peptide deimination by peptidylarginine deiminase-4
Biol. Chem.
390
99-107
2009
Homo sapiens
Manually annotated by BRENDA team
Loos, T.; Mortier, A.; Gouwy, M.; Ronsse, I.; Put, W.; Lenaerts, J.P.; Van Damme, J.; Proost, P.
Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
Blood
112
2648-2656
2008
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Musse, A.A.; Li, Z.; Ackerley, C.A.; Bienzle, D.; Lei, H.; Poma, R.; Harauz, G.; Moscarello, M.A.; Mastronardi, F.G.
Peptidylarginine deiminase 2 (PAD2) overexpression in transgenic mice leads to myelin loss in the central nervous system
Dis. Model. Mech.
1
229-240
2008
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Ying, S.; Dong, S.; Kawada, A.; Kojima, T.; Chavanas, S.; Mechin, M.C.; Adoue, V.; Serre, G.; Simon, M.; Takahara, H.
Transcriptional regulation of peptidylarginine deiminase expression in human keratinocytes
J. Dermatol. Sci.
53
2-9
2009
Homo sapiens (Q6TGC4), Homo sapiens (Q9ULC6), Homo sapiens (Q9ULW8), Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Proost, P.; Loos, T.; Mortier, A.; Schutyser, E.; Gouwy, M.; Noppen, S.; Dillen, C.; Ronsse, I.; Conings, R.; Struyf, S.; Opdenakker, G.; Maudgal, P.C.; Van Damme, J.
Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
J. Exp. Med.
205
2085-2097
2008
Oryctolagus cuniculus, Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Li, P.; Yao, H.; Zhang, Z.; Li, M.; Luo, Y.; Thompson, P.R.; Gilmour, D.S.; Wang, Y.
Regulation of p53 target gene expression by peptidylarginine deiminase 4
Mol. Cell. Biol.
28
4745-4758
2008
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Abdeen, S.M.; Olusi, S.O.
Peptidyl arginine deiminase: A novel immunohistochemical marker for liver fibrosis in patients with chronic hepatitis
Acta Histochem.
112
592-603
2010
Homo sapiens
Manually annotated by BRENDA team
Knuckley, B.; Causey, C.P.; Jones, J.E.; Bhatia, M.; Dreyton, C.J.; Osborne, T.C.; Takahara, H.; Thompson, P.R.
Substrate specificity and kinetic studies of PADs 1, 3, and 4 identify potent and selective inhibitors of protein arginine deiminase 3
Biochemistry
49
4852-4863
2010
Homo sapiens
Manually annotated by BRENDA team
Knuckley, B.; Causey, C.P.; Pellechia, P.J.; Cook, P.F.; Thompson, P.R.
Haloacetamidine-based inactivators of protein arginine deiminase 4 (PAD4): evidence that general acid catalysis promotes efficient inactivation
ChemBioChem
11
161-165
2010
Homo sapiens
Manually annotated by BRENDA team
Jones, J.E.; Causey, C.P.; Knuckley, B.; Slack-Noyes, J.L.; Thompson, P.R.
Protein arginine deiminase 4 (PAD4): Current understanding and future therapeutic potential
Curr. Opin. Drug Discov. Devel.
12
616-627
2009
Homo sapiens
Manually annotated by BRENDA team
Jang, B.; Jeon, Y.C.; Choi, J.K.; Park, M.; Kim, J.I.; Ishigami, A.; Maruyama, N.; Carp, R.I.; Kim, Y.S.; Choi, E.K.
Peptidylarginine deiminase modulates the physiological roles of enolase via citrullination: links between altered multifunction of enolase and neurodegenerative diseases
Biochem. J.
445
183-192
2012
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Slack, J.L.; Jones, L.E.; Bhatia, M.M.; Thompson, P.R.
Autodeimination of protein arginine deiminase 4 alters protein-protein interactions but not activity
Biochemistry
50
3997-4010
2011
Homo sapiens
Manually annotated by BRENDA team
Rose, R.; Rose, M.; Ottmann, C.
Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI
J. Struct. Biol.
180
65-72
2012
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.L.; Chiang, Y.H.; Liu, G.Y.; Hung, H.C.
Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4)
PLoS ONE
6
e21314
2011
Homo sapiens
Manually annotated by BRENDA team
Unno, M.; Kizawa, K.; Ishihara, M.; Takahara, H.
Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type III
Acta Crystallogr. Sect. F
68
668-670
2012
Homo sapiens (Q9ULW8), Homo sapiens
Manually annotated by BRENDA team
Unno, M.; Kinjo, S.; Kizawa, K.; Takahara, H.
Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type I
Acta Crystallogr. Sect. F
69
1357-1359
2013
Homo sapiens (Q9ULC6), Homo sapiens
Manually annotated by BRENDA team
Darrah, E.; Rosen, A.; Giles, J.; Andrade, F.
Peptidylarginine deiminase 2, 3 and 4 have distinct specificities against cellular substrates: Novel insights into autoantigen selection in rheumatoid arthritis
Ann. Rheum. Dis.
71
92-98
2012
Homo sapiens (Q9ULW8), Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Dreyton, C.J.; Knuckley, B.; Jones, J.E.; Lewallen, D.M.; Thompson, P.R.
Mechanistic studies of protein arginine deiminase 2: evidence for a substrate-assisted mechanism
Biochemistry
53
4426-4433
2014
Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Assohou-Luty, C.; Raijmakers, R.; Benckhuijsen, W.E.; Stammen-Vogelzangs, J.; de Ru, A.; van Veelen, P.A.; Franken, K.L.; Drijfhout, J.W.; Pruijn, G.J.
The human peptidylarginine deiminases type 2 and type 4 have distinct substrate specificities
Biochim. Biophys. Acta
1844
829-836
2014
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Bozdag, M.; Dreker, T.; Henry, C.; Tosco, P.; Vallaro, M.; Fruttero, R.; Scozzafava, A.; Carta, F.; Supuran, C.T.
Novel small molecule protein arginine deiminase 4 (PAD4) inhibitors
Bioorg. Med. Chem. Lett.
23
715-719
2013
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Jamali, H.; Khan, H.A.; Stringer, J.R.; Chowdhury, S.; Ellman, J.A.
Identification of multiple structurally distinct, nonpeptidic small molecule inhibitors of protein arginine deiminase 3 using a substrate-based fragment method
J. Am. Chem. Soc.
137
3616-3621
2015
Homo sapiens (Q9ULW8)
Manually annotated by BRENDA team
Subramanian, V.; Knight, J.S.; Parelkar, S.; Anguish, L.; Coonrod, S.A.; Kaplan, M.J.; Thompson, P.R.
Design, synthesis, and biological evaluation of tetrazole analogs of Cl-amidine as protein arginine deiminase inhibitors
J. Med. Chem.
58
1337-1344
2015
Homo sapiens (Q9ULC6), Homo sapiens (Q9ULW8), Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Slade, D.J.; Fang, P.; Dreyton, C.J.; Zhang, Y.; Fuhrmann, J.; Rempel, D.; Bax, B.D.; Coonrod, S.A.; Lewis, H.D.; Guo, M.; Gross, M.L.; Thompson, P.R.
Protein arginine deiminase 2 binds calcium in an ordered fashion implications for inhibitor design
ACS Chem. Biol.
10
1043-1053
2015
Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Jamali, H.; Khan, H.A.; Tjin, C.C.; Ellman, J.A.
Cellular activity of new small molecule protein arginine deiminase 3 (PAD3) inhibitors
ACS Med. Chem. Lett.
7
847-851
2016
Homo sapiens (Q9ULW8), Homo sapiens
Manually annotated by BRENDA team
Kunieda, K.; Kawaguchi, M.; Ieda, N.; Nakagawa, H.
Development of a highly sensitive fluorescence probe for peptidyl arginine deiminase (PAD) activity
Bioorg. Med. Chem. Lett.
29
923-928
2019
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Teo, C.Y.; Tejo, B.A.; Leow, A.T.C.; Salleh, A.B.; Abdul Rahman, M.B.
Novel furan-containing peptide-based inhibitors of protein arginine deiminase type IV (PAD4)
Chem. Biol. Drug Des.
90
1134-1146
2017
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Olson, J.S.; Lubner, J.M.; Meyer, D.J.; Grant, J.E.
An in silico analysis of primary and secondary structure specificity determinants for human peptidylarginine deiminase types 2 and 4
Comput. Biol. Chem.
70
107-115
2017
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Zhou, Y.; Mittereder, N.; Sims, G.
Perspective on protein arginine deiminase activity-bicarbonate is a pH-independent regulator of citrullination
Front. Immunol.
9
34
2018
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8)
Manually annotated by BRENDA team
Trabocchi, A.; Pala, N.; Krimmelbein, I.; Menchi, G.; Guarna, A.; Sechi, M.; Dreker, T.; Scozzafava, A.; Supuran, C.; Carta, F.
Peptidomimetics as protein arginine deiminase 4 (PAD4) inhibitors
J. Enzyme Inhib. Med. Chem.
30
466-471
2015
Homo sapiens (Q9UM07)
Manually annotated by BRENDA team
Damgaard, D.; Bjorn, M.E.; Jensen, P.O.; Nielsen, C.H.
Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase
J. Enzyme Inhib. Med. Chem.
32
1203-1208
2017
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Subramanian, V.; Knight, J.S.; Parelkar, S.; Anguish, L.; Coonrod, S.A.; Kaplan, M.J.; Thompson, P.R.
Design, synthesis, and biological evaluation of tetrazole analogs of Cl-amidine as protein arginine deiminase inhibitors
J. Med. Chem.
58
1337-1344
2015
Homo sapiens (Q9UM07), Homo sapiens (Q9Y2J8), Homo sapiens
Manually annotated by BRENDA team
Saijo, S.; Nagai, A.; Kinjo, S.; Mashimo, R.; Akimoto, M.; Kizawa, K.; Yabe-Wada, T.; Shimizu, N.; Takahara, H.; Unno, M.
Monomeric form of peptidylarginine deiminase type I revealed by X-ray crystallography and small-angle X-ray scattering
J. Mol. Biol.
428
3058-3073
2016
Homo sapiens (Q9ULC6), Homo sapiens
Manually annotated by BRENDA team
Lee, C.; Lin, C.; Liu, Y.; Liu, G.; Liu, J.; Hung, H.
Molecular interplay between the dimer interface and the substrate-binding site of human peptidylarginine deiminase 4
Sci. Rep.
7
42662
2017
Homo sapiens (Q9UM07), Homo sapiens
Manually annotated by BRENDA team