Arginine deiminase
| arginine deiminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.3.6 | ||||||||
| CAS no. | 9027-98-9 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction
- L-arginine + H2O L-citrulline + NH3
Thus, the two substrates of this enzyme are L-arginine and H2O, whereas its two products are 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 L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors.
Recently, a new enzyme that catalyzes the chemical reaction
- L-arginine + 2H2O L-ornithine + 2NH3 + CO2 was identified in cyanobacteria[1] which should be named as arginine dihydrolase.
Structural studies
[edit]As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1LXY, 1RXX, 1S9R, 2A9G, 2AAF, 2ABR, and 2ACI.
References
[edit]- OGINSKY EL, GEHRIG RF (1952). "The arginine dihydrolase system of Streptococcus faecalis. II Properties of arginine desimidase". J. Biol. Chem. 198 (2): 799–805. doi:10.1016/S0021-9258(18)55537-X. PMID 12999797.
- LIU Y, BURNE RA (2009). "Multiple two-component systems modulate alkali generation in Streptococcus gordonii in response to environmental stresses". J. Bacteriol. 191 (23): 7353–7362. doi:10.1128/JB.01053-09. PMC 2786566. PMID 19783634.
- PETRAK B, SULLIAN L, RETARN S (1957). "Behavior of purified arginine deiminase from S. faecalis". Arch. Biochem. Biophys. 69: 186–197. doi:10.1016/0003-9861(57)90485-X. PMID 13445192.
- RATNER S (1954). "Urea Synthesis and Metabolism of Arginine and Citrulline". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 15. pp. 319–87. doi:10.1002/9780470122600.ch8. ISBN 9780470122600. PMID 13158183.
{{cite book}}:|journal=ignored (help) - LIU Y, BURNE RA (2008). "Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes". Appl Environ Microbiol. 74 (16): 5023–5030. Bibcode:2008ApEnM..74.5023L. doi:10.1128/AEM.00556-08. PMC 2519279. PMID 18552185.
