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Literature summary extracted from

  • Vega, M.C.; Zou, P.; Fernandez, F.J.; Murphy, G.E.; Sterner, R.; Popov, A.; Wilmanns, M.
    Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit (2005), Mol. Microbiol., 55, 675-686.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.17 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 (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.17 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

EC Number Inhibitors Comment Organism Structure
2.4.2.17 histidine noncompetitive feedback inhibition Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.17 additional information
-
 additional information steady-state kinetics Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.17 Mg2+ dependent on Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.17 200000 220000 gel filtration Thermotoga maritima

Natural Substrates/ Products (Substrates)

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 Thermotoga maritima first step in histidine biosynthesis, mechanism of regulation, overview 1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.17 Thermotoga maritima
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.17 recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ from Escherichia coli in a multistep procedure Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.17 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermotoga maritima 1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
 r
2.4.2.17 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
2.4.2.17 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

EC Number Subunits Comment Organism
2.4.2.17 More subunit structures, structure evolution Thermotoga maritima
2.4.2.17 octamer 4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4 Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
2.4.2.17 ATP phosphoribosyl transferase
-
 Thermotoga maritima
2.4.2.17 ATP phosphoribosyl transferase complex
-
 Thermotoga maritima
2.4.2.17 ATP-PRTase
-
 Thermotoga maritima
2.4.2.17 N-1-(5'-phosphoribosyl)-ATP transferase
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.17 20
-
 assay at Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.17 8
-
 assay at Thermotoga maritima