In enzymology, a protein-arginine deiminase (PAD) (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 ⇌ {\displaystyle \rightleftharpoons } 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 PDB: 1WD8, PDB: 1WD9, PDB: 1WDA, PDB: 2DEW, PDB: 2DEX, PDB: 2DEY, and PDB: 2DW5.
Mammalian proteins Mammals have 5 protein-arginine deiminases, with symbols
PADI1, PADI2, PADI3, PADI4, PADI6 except for rodents, there the letter case is different:
Padi1, Padi2, Padi3, Padi4, Padi6 The different case is just a historical artifact. It doesn't indicate that the rodent proteins are special.
Inhibitors Irreversible inhibitors
Cl-amidine, BB-Cl-Amidine, YW3-56 Reversible inhibitors
GSK484, GSK199
References
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)



