Arginine decarboxylase
| arginine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.19 | ||||||||
| CAS no. | 9024-77-5 | ||||||||
| 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 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
- Blethen SL, Boeker EA, Snell EE (1968). "Argenine [sic] decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme". J. Biol. Chem. 243 (8): 1671–7. PMID 4870599.
- Ramakrishna S, Adiga PR (1975). "Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties". Eur. J. Biochem. 59 (2): 377–86. doi:10.1111/j.1432-1033.1975.tb02465.x. PMID 1252.
- Taylor ES, Gale EF (1945). "Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors". Biochem. J. 39 (1): 52–58. PMC 1258148. PMID 16747854.
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