Protein-arginine deiminase
| 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 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.
See also
References
- Fujisaki M, Sugawara K. "Properties of peptidylarginine deiminase from the epidermis of newborn rats". J. Tokyo. Biochem. (1): 257–63. PMID 7217033.
- protein-arginine deiminase at the US National Library of Medicine Medical Subject Headings (MeSH)
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