Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway.
Mathews, I.I., Kappock, T.J., Stubbe, J., Ealick, S.E.(1999) Structure 7: 1395-1406
- PubMed: 10574791 
- DOI: https://doi.org/10.1016/s0969-2126(00)80029-5
- Primary Citation of Related Structures:  
1D7A, 1QCZ - PubMed Abstract: 
Conversion of 5-aminoimidazole ribonucleotide (AIR) to 4-carboxyaminoimidazole ribonucleotide (CAIR) in Escherichia coli requires two proteins - PurK and PurE. PurE has recently been shown to be a mutase that catalyzes the unusual rearrangement of N(5)-carboxyaminoimidazole ribonucleotide (N(5)-CAIR), the PurK reaction product, to CAIR. PurEs from higher eukaryotes are homologous to E. coli PurE, but use AIR and CO(2) as substrates to produce CAIR directly.
Organizational Affiliation: 
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.