Arginine decarboxylase

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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

  • 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 decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme". J. Biol. Chem. 243: 1671&ndash, 7. PMID 4870599.
  • Ramakrishna S, Adiga PR (1975). "Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properites". Eur. J. Biochem. 59: 377&ndash, 86. 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&ndash, 58.

External links

The CAS registry number for this enzyme class is 9024-77-5.

Gene Ontology (GO) codes


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