Protein-arginine deiminase

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In enzymology, a protein-arginine deiminase (EC 3.5.3.15) is an enzyme that catalyzes the chemical reaction

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.

References

  • IUBMB entry for 3.5.3.15
  • BRENDA references for 3.5.3.15 (Recommended.)
  • PubMed references for 3.5.3.15
  • PubMed Central references for 3.5.3.15
  • Google Scholar references for 3.5.3.15
  • Fujisaki M, Sugawara K (Tokyo). "Properties of peptidylarginine deiminase from the epidermis of newborn rats". J. Biochem.: 257&ndash, 63. PMID 7217033. Check date values in: |date= (help)

External links

The CAS registry number for this enzyme class is 75536-80-0.

Gene Ontology (GO) codes


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