| 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
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
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
- ^ 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)
This page was last edited on 3 December 2023, at 17:17