Cloned (Comment) | Organism |
---|---|
separate expression of subunits HisGs and HisZ in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled proteins | Thermotoga maritima |
Crystallization (Comment) | Organism |
---|---|
purified recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ separately, in a binary complex with histidine, sitting drop vapour diffusion method, 0.002 ml of 8 mg/ml protein mixed with 0.002 ml reservoir solution containing 22.5% w/v methyl-2,4-pentanediol, 0.2 M phosphate/citrate buffer, pH 4.2, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling | Thermotoga maritima |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
histidine | noncompetitive feedback inhibition | Thermotoga maritima |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics | Thermotoga maritima |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | dependent on | Thermotoga maritima |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
200000 | 220000 | gel filtration | Thermotoga maritima |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | Thermotoga maritima | first step in histidine biosynthesis, mechanism of regulation, overview | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ from Escherichia coli in a multistep procedure | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermotoga maritima | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
r | |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | first step in histidine biosynthesis, mechanism of regulation, overview | Thermotoga maritima | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
r | |
additional information | the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ, only the complete hetero-octameric complex is catalytically active, the complex possesses 8 histidine binding sites at the subunit interfaces and histidine as a ligand | Thermotoga maritima | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | subunit structures, structure evolution | Thermotoga maritima |
octamer | 4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4 | Thermotoga maritima |
Synonyms | Comment | Organism |
---|---|---|
ATP phosphoribosyl transferase | - |
Thermotoga maritima |
ATP phosphoribosyl transferase complex | - |
Thermotoga maritima |
ATP-PRTase | - |
Thermotoga maritima |
N-1-(5'-phosphoribosyl)-ATP transferase | - |
Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Thermotoga maritima |