Arginine decarboxylase

From Wikipedia, the free encyclopedia

In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction

L-arginine $\rightleftharpoons$ 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.

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

[edit] 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.

[edit] References

IUBMB entry for 4.1.1.19
BRENDA references for 4.1.1.19 (Recommended.)
PubMed references for 4.1.1.19
PubMed Central references for 4.1.1.19
Google Scholar references for 4.1.1.19
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: 1671–7. PMID 4870599.
Ramakrishna S, Adiga PR (1975). "Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properites". Eur. J. Biochem. 59: 377–86. doi:10.1111/j.1432-1033.1975.tb02465.x. PMID 1252.
Taylor ES and Gale EF (1945). "Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors". Biochem. J. 39: 52–58.