| protein-arginine deiminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Protein-arginine deiminase 4, dimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 3.5.3.15 | ||||||||
| CAS no. | 75536-80-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a protein-arginine deiminase (EC 3.5.3.15) is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination:
- protein L-arginine + H2O protein L-citrulline + NH3
Thus, the two substrates of this enzyme are protein L-arginine (arginine residue inside a protein) and H2O, whereas its two products are protein L-citrulline and NH3:
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is protein-L-arginine iminohydrolase. This enzyme is also called peptidylarginine deiminase.
Structural studies[edit]
As of late 2007, seven structures have been solved for this class of enzymes, with PDB accession codes 1WD8, 1WD9, 1WDA, 2DEW, 2DEX, 2DEY, and 2DW5.
Mammalian proteins[edit]
Mammals have 5 protein-arginine deiminases, with symbols
except for rodents, there the letter case is different:
- Padi1, Padi2, Padi3, Padi4, Padi6[3]
The different case is just a historical artifact. It doesn't indicate that the rodent proteins are special.
References[edit]
- ^ Sams, K.L; Mukai, C; Marks, B.A; Mittal, C; Demeter, E.A; Nelissen, S; Grenier, J.K; Tate, A.E; Ahmed, F; Coonrod, S.A (October 2022). "Delayed puberty, gonadotropin abnormalities and subfertility in male Padi2/Padi4 double knockout mice". Reprod Biol Endocrinol. 20 (1): 150. doi:10.1186/s12958-022-01018-w. PMC 9555066. PMID 36224627.
- ^ "Search results for "peptidyl arginine deiminase"". Vertebrate Gene Nomenclature Committee. Retrieved 9 February 2022.
- ^ "Protein Superfamily Detail: Protein-arginine_deiminase". Mouse Genome Informatics.
- Fujisaki M, Sugawara K (January 1981). "Properties of peptidylarginine deiminase from the epidermis of newborn rats". J. Biochem. 89 (1). Tokyo: 257–63. doi:10.1093/oxfordjournals.jbchem.a133189. PMID 7217033.
- protein-arginine+deiminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
