Protein-arginine deiminase

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Template:Infobox enzyme In enzymology, a protein-arginine deiminase (Template:EC number) 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:

The chemical conversion of arginine to citrulline, known as citrullination or deimination.

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 Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

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

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Template:Carbon-nitrogen non-peptide hydrolases Template:Enzymes Template:Portal bar


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