Protein-arginine deiminase

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protein-arginine deiminase
Identifiers
EC number 3.5.3.15
CAS number 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 / EGO

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 \rightleftharpoons 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[edit]

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[edit]

References[edit]