Protein-arginine deiminase

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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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 1WD8, 1WD9, 1WDA, 2DEW, 2DEX, 2DEY, and 2DW5.

Mammalian proteins[]

Mammals have 5 protein-arginine deiminases, with symbols

• PADI1, PADI2, PADI3, PADI4, ^[1]

except for rodents, there the letter case is different:

• Padi1, Padi2, Padi3, Padi4, Padi6^[2]

The different case is just a historical artifact. It doesn't indicate that the rodent proteins are special.

References[]

• Fujisaki M, Sugawara K (January 1981). "Properties of peptidylarginine deiminase from the epidermis of newborn rats". J. Biochem. Tokyo. 89 (1): 257–63. doi:10.1093/oxfordjournals.jbchem.a133189. PMID 7217033.
• protein-arginine+deiminase at the US National Library of Medicine Medical Subject Headings (MeSH)