| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| KCl | dependent on | Acinetobacter baumannii |
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Acinetobacter baumannii |
| Protein Variants | Comment | Organism |
|---|---|---|
| R70A | the mutation causes an about 5fold decrease in kcat compared to the wild type enzyme and nullifies the higher enzyme kcat with ADP as substrate observed with the wild type variant at 25°C | Acinetobacter baumannii |
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.111 | - |
1-(5-phospho-beta-D-ribosyl)-ATP | at pH 8.5 and 5°C | Acinetobacter baumannii | |
| 0.23 | - |
ATP | at pH 8.5 and 5°C | Acinetobacter baumannii |
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | Acinetobacter baumannii | |
| Mn2+ | kcat is enhanced when Mn2+ replaces Mg2+ as the divalent metal | Acinetobacter baumannii |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Acinetobacter baumannii | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| ATP + 5-phospho-alpha-D-ribose 1-diphosphate | Acinetobacter baumannii | - |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
r |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter baumannii | A0A7U3XWM9 AND B2HWK9 | subunits HisG and HisZ | - |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Acinetobacter baumannii | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Acinetobacter baumannii | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
r |
| Synonyms | Comment | Organism |
|---|---|---|
| ATPPRT | the enzyme is a multi-protein complex where the regulatory protein HisZ allosterically enhances catalysis by the catalytic protein HisGS | Acinetobacter baumannii |
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.95 | - |
1-(5-phospho-beta-D-ribosyl)-ATP | at pH 8.5 and 5°C | Acinetobacter baumannii | |
| 2.95 | - |
ATP | at pH 8.5 and 5°C | Acinetobacter baumannii |
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13 | - |
ATP | at pH 8.5 and 5°C | Acinetobacter baumannii | |
| 27 | - |
1-(5-phospho-beta-D-ribosyl)-ATP | at pH 8.5 and 5°C | Acinetobacter baumannii |