EC Number   |
Title |
Organism |
|---|
    5.4.99.18 | Identification of B. anthracis N(5)-carboxyaminoimidazole ribonucleotide mutase (PurE) active site binding compounds via fragment library screening |
Bacillus anthracis |
| 5.4.99.18 | Identification of Bacillus anthracis PurE inhibitors with antimicrobial activity |
Bacillus anthracis |
| 5.4.99.18 | Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE) |
Acetobacter aceti |
| 5.4.99.18 | Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti |
Acetobacter aceti |
| 5.4.99.18 | Crystal structure of a phosphoribosylaminoimidazole mutase PurE from Thermotoga maritima at 1.77 A resolution |
Thermotoga maritima |
| 5.4.99.18 | Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway |
Escherichia coli |
| 5.4.99.18 | Evidence for the Direct Transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase |
Escherichia coli |
| 5.4.99.18 | Genomic organization of purK and purE in Brevibacterium ammoniagenes ATCC 6872: purE locus provides a clue for genomic evolution |
Corynebacterium ammoniagenes |
| 5.4.99.18 | Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis |
Escherichia coli |
| 5.4.99.18 | Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis |
Escherichia coli NK6051 |
