PMID:10574791
| Citation |
Mathews, II, Kappock, TJ, Stubbe, J and Ealick, SE (1999) Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway. Structure 7:1395-406 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Carboxy-Lyases/chemistry; Carboxy-Lyases/metabolism; Crystallography, X-Ray; Escherichia coli/chemistry; Models, Molecular; Molecular Sequence Data; Protein Conformation; Purines/biosynthesis; Sequence Homology, Amino Acid |
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