Protein-arginine deiminase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
protein-arginine deiminase
5n0m.jpg
Protein-arginine deiminase 4, dimer, Human
Identifiers
EC number3.5.3.15
CAS number75536-80-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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[edit]

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.

See also[edit]

References[edit]

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