Cloned (Comment) | Organism |
---|---|
expression of selenomethionine-labeled enzyme in strain B834(DE3) | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | binding structure and inhibition mode | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for substrate binding | 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, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P60757 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant selenomethionine-labeled enzyme from strain B834(DE3) | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate | substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction 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, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway | Escherichia coli | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | quarternary structure | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ATP-phosphoribosyltransferase | - |
Escherichia coli |
ATP-PRT | - |
Escherichia coli |