EC number:3.5.3.15

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.3 In linear amidines
ID:3.5.3.15
Description:Protein-arginine deiminase.
Alternative Name: PAD.
Cath: 3.75.10.10; 2.60.40.1700; 2.60.40.1860;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.3.15
BRENDA Enzyme Link: BRENDA 3.5.3.15
KEGG Enzyme Link: KEGG3.5.3.15
BioCyc Enzyme Link: BioCyc 3.5.3.15
ExPASy Enzyme Link: ExPASy3.5.3.15
EC2PDB Enzyme Link: EC2PDB 3.5.3.15
ExplorEnz Enzyme Link: ExplorEnz 3.5.3.15
PRIAM enzyme-specific profiles Link: PRIAM 3.5.3.15
IntEnz Enzyme Link: IntEnz 3.5.3.15
MEDLINE Enzyme Link: MEDLINE 3.5.3.15

EC number:3.5.3.15

MSA:

3.5.3.15;
Phylogenetic Tree:

3.5.3.15;
Uniprot:
M-CSA:
RHEA:18089 H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](-[NH2;+0:3])=[NH;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](-[NH2;+0:4])=[O;H0;+0:5].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Properties of peptidylarginine deiminase from the epidermis of newborn rats.Fujisaki M, Sugawara K1981 Jan7217033
Structural and biochemical analyses of the human PAD4 variant encoded by a functional haplotype gene.Horikoshi N, Tachiwana H, Saito K, Osakabe A, Sato M, Yamada M, Akashi S, Nishimura Y, Kagawa W, Kurumizaka H2011 Feb21245532
Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4.Arita K, Shimizu T, Hashimoto H, Hidaka Y, Yamada M, Sato M2006 Apr 416567635