Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation | Escherichia coli | |
ATP | inhibits the reaction at high concentrations | Escherichia coli | |
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 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | Escherichia coli | first step in histidine biosynthesis | diphosphate + N-1-(5'-phosphoribosyl)-ATP | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate | double displacement mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Escherichia coli | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
? | |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | first step in histidine biosynthesis | Escherichia coli | diphosphate + N-1-(5'-phosphoribosyl)-ATP | - |
? |