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Literature summary for 6.3.4.18 extracted from
- Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (2014), Acta Crystallogr. Sect. D, 70, 3057-3065 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Bacillus anthracis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures with various combinations of ATP, ADP, Mg2+, hydrogencarbonate and aminoimidazole ribonucleotide in the active site. The binding involves interactions with the conserved residues Arg272, His274 and Lys348. The formation of a carboxyphosphate intermediate through ATP phosphoryl transfer is proposed, followed by carboxylation of AIR to give the product | Bacillus anthracis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | Q81ZH7 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PurK | - |
Bacillus anthracis |
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