Arginine deiminase

From Wikipedia, the free encyclopedia

In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction

L-arginine + H₂O $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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.

[edit] References

IUBMB entry for 3.5.3.6
BRENDA references for 3.5.3.6 (Recommended.)
PubMed references for 3.5.3.6
PubMed Central references for 3.5.3.6
Google Scholar references for 3.5.3.6
OGINSKY EL, GEHRIG RF (1952). "The arginine dihydrolase system of Streptococcus faecalis. II Properties of arginine desimidase". J. Biol. Chem. 198: 799–805. PMID 12999797.
Petrack B, Sullivan L and Ratner S (1957). "Behavior of purified arginine desiminase from S. faecalis". Arch. Biochem. Biophys. 69: 186–197.
RATNER S (1954). "Urea synthesis and metabolism of arginine and citrulline". Adv. Enzymol. Relat. Subj. Biochem. 15: 319–87. PMID 13158183.