EC - Phosphoribosylaminoimidazole carboxylase

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IntEnz Enzyme Nomenclature


Accepted name:
phosphoribosylaminoimidazole carboxylase
Other names:
5-phosphoribosyl-5-aminoimidazole carboxylase
5-amino-1-ribosylimidazole 5-phosphate carboxylase
AIR carboxylase
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase
class II PurE
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
Systematic name:
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]



While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC, 5-(carboxyamino)imidazole ribonucleotide synthase and EC, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50975
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043727 , GO:0004638
CAS Registry Number: 9032-04-6
UniProtKB/Swiss-Prot: (20) [show] [UniProt]


  1. Lukens, L.N. and Buchanan, J.M.
    Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from 5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide.
    J. Biol. Chem. 234: 1799-1805 (1959). [PMID: 13672967]
  2. Firestine, S.M., Poon, S.W., Mueller, E.J., Stubbe, J. and Davisson, V.J.
    Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.
    Biochemistry 33: 11927-11934 (1994). [PMID: 7918411]
  3. Firestine, S. M., Misialek, S., Toffaletti, D.L., Klem, T.J., Perfect, J.R. and Davisson, V.J.
    Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis.
    Arch. Biochem. Biophys. 351: 123-134 (1998). [PMID: 9500840]

[EC created 1961, modified 2000, modified 2006]