EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.2.17 | AMP | linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation | Escherichia coli | |
2.4.2.17 | ATP | inhibits the reaction at high concentrations | Escherichia coli | |
2.4.2.17 | L-histidine | feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.17 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | Escherichia coli | first step in histidine biosynthesis | diphosphate + N-1-(5'-phosphoribosyl)-ATP | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.2.17 | Escherichia coli | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate | sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes | Escherichia coli | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate | double displacement mechanism | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.17 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Escherichia coli | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
? | |
2.4.2.17 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | first step in histidine biosynthesis | Escherichia coli | diphosphate + N-1-(5'-phosphoribosyl)-ATP | - |
? |