Arginine decarboxylase
arginine decarboxylase | |||||||||
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Identifiers | |||||||||
EC number | 4.1.1.19 | ||||||||
CAS number | Template:CAS | ||||||||
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 | ||||||||
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In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction
- L-arginine agmatine + CO2
Hence, this enzyme has one substrate, L-arginine, and two products, agmatine and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-arginine carboxy-lyase (agmatine-forming). Other names in common use include SpeA, and L-arginine carboxy-lyase. This enzyme participates in urea cycle and metabolism of amino groups and glutamate metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1MT1, 1N13, 1N2M, 2NV9, and 2NVA.
References
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