Protein-arginine deiminase

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 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, 7 structures have been solved for this class of enzymes, with PDB accession codes 1WD8, 1WD9, 1WDA, 2DEW, 2DEX, 2DEY, and 2DW5.

See also

• PADI1
• PADI2
• PADI3
• PADI4

References

• Fujisaki M, Sugawara K. "Properties of peptidylarginine deiminase from the epidermis of newborn rats". J. (Tokyo). Biochem. (1): 257–63. PMID 7217033. 
• protein-arginine deiminase at the US National Library of Medicine Medical Subject Headings (MeSH)