Arginine deiminase

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arginine deiminase
Identifiers
EC number 3.5.3.6
CAS number 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 / EGO

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. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors.

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]