| EC |
6.3.4.18 |
| Accepted name: |
5-(carboxyamino)imidazole ribonucleotide synthase |
| Reaction: |
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole |
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For diagram of the late stages of purine biosynthesis, click here |
| Other name(s): |
N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK |
| Systematic name: |
5-amino-1-(5-phospho-D-ribosyl)imidazole:carbon-dioxide ligase (ADP-forming) |
| Comments: |
In Escherichia coli, this enzyme, along with EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. Belongs to the ATP grasp protein superfamily [3]. Carboxyphosphate is the putative acyl phosphate intermediate. Involved in the late stages of purine biosynthesis. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 255379-40-9 |
| References: |
| 1. |
Meyer, E., Leonard, N.J., Bhat, B., Stubbe, J. and Smith, J.M. Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway. Biochemistry 31 (1992) 5022–5032. [PMID: 1534690] |
| 2. |
Mueller, E.J., Meyer, E., Rudolph, J., Davisson, V.J. and Stubbe, J. N5-Carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coli. Biochemistry 33 (1994) 2269–2278. [PMID: 8117684] |
| 3. |
Thoden, J.B., Kappock, T.J., Stubbe, J. and Holden, H.M. Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide
synthetase: a member of the ATP grasp protein superfamily. Biochemistry 38 (1999) 15480–15492. [DOI] [PMID: 10569930] |
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| [EC 6.3.4.18 created 2006] |
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