Protein-arginine deiminase


In enzymology, a protein-arginine deiminase is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination:
Thus, the two substrates of this enzyme are protein L-arginine 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,,,,,, and.

Mammalian proteins

Mammals have 5 protein-arginine deiminases, with symbols
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
Reversible inhibitors