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Information on EC 3.5.3.15 - protein-arginine deiminase and Organism(s) Rattus norvegicus and UniProt Accession P20717
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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 taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deiminase, protein (arginine)
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HL-60 PAD
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-
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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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-
-
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peptidylarginine deiminase
Peptidylarginine deiminase type alpha
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-
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protein arginine deiminase
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-
-
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PAD
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peptidylarginine deiminase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY
75536-80-0
-
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
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
-
-
ir
benzoyl-Arg ethyl ester + H2O
benzoyl-citrulline ethyl ester + 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
-
-
-
-
?
keratin + H2O
? + NH3
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peptidylarginine deiminase type I acts on the arginine residue in the V2 subdomain of mouse keratin more readily than peptidylarginine deiminase type II
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-
?
protein L-Arg + H2O
?
-
all-trans retinoic acid increases peptidylarginine deiminase activity in a newborn rat keratinocyte cell line
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-
?
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
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-
?
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
-
-
ir
protein-L-arginine + H2O
protein-L-citrulline + NH3
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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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-
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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
?
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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
?
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PAD2 is involved in some processes of neurodegeneration and myelination in the central nervous system
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-
?
additional information
?
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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
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-
?
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
?
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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
?
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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
-
-
?
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
protein-L-arginine + H2O
protein-L-citrulline + NH3
-
-
-
ir
additional information
?
-
-
PAD2 is involved in some processes of neurodegeneration and myelination in the central nervous system
-
-
?
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-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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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embryonal, isozyme expression analysis, PAD2 expression occurs also in 19- to 21-day-old embryos at a developmental stage well before myelination begins, overview
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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
additional information
additional information
-
no activity detected in spleen, stomach, small intestine, large intestine, pancreas, serum and heart
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PADI2_RAT
665
0
75356
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujisaki, M.; Sugawara, K.
Properties of peptidylarginine deiminase from the epidermis of newborn rats
J. Biochem.
89
257-263
1981
Rattus norvegicus
Kubilus, J.; Baden, H.P.
Purification and properties of a brain enzyme which deiminates proteins
Biochim. Biophys. Acta
745
285-291
1983
Bos taurus, Rattus norvegicus
Rothnagel, J.A.; Rogers, G.E.
Citrulline in proteins from the enzymatic deimination of arginine residues
Methods Enzymol.
107
624-631
1984
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Rattus norvegicus
Nishijo, T.; Kawada, A.; Kanno, T.; Shiraiwa, M.; Takahara, H.
Isolation and molecular cloning of epidermal- and hair follicle-specific peptidylarginine deiminase (type III) from rat
J. Biochem.
121
868-875
1997
Rattus norvegicus
Nagata, S.; Senshu, T.
Peptidylarginine deiminase in rat and mouse hemopoietic cells
Experientia
46
72-74
1990
Mus musculus, Rattus norvegicus
Senshu, T.; Akiyama, K.; Ishigami, A.; Nomura, K.
Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1
J. Dermatol. Sci.
21
113-126
1999
Rattus norvegicus
Ishigami, A.; Ohsawa, T.; Watanabe, K.; Senshu, T.
all-trans Retinoic acid increases peptidylarginine deiminase in a newborn keratinocyte cell line
Biochem. Biophys. Res. Commun.
223
299-303
1996
Rattus norvegicus
Asaga, H.; Ishigami, A.
Microglial expression of peptidylarginine deiminase 2 in the prenatal rat brain
Cell. Mol. Biol. Lett.
12
536-544
2007
Rattus norvegicus
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
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)
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