Protein-arginine deiminase
From Wikipedia, the free encyclopedia
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.
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[edit] 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.
[edit] 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.: 257–63. PMID 7217033.
[edit] External links
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- The CAS registry number for this enzyme class is 75536-80-0.