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Literature summary for 2.7.6.1 extracted from

  • Arnvig, K.; Hove-Jensen, B.; Switzer, R.L.
    Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis (1990), Eur. J. Biochem., 192, 195-200.
    View publication on PubMed
Search for more literature for 2.7.6.1

Activating Compound

Activating Compound Comment Organism Structure
phosphate requirement Bacillus subtilis
phosphate the optimum concentration at pH 8.2 is 50-60 mM, higher concentrations are inhibitory Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

General Stability

General Stability Organism
relatively stable in absence of phosphate Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
ADP the most effective Bacillus subtilis
AMP 68% inhibition at 5 mM Bacillus subtilis
ATP moderate inhibition above 3 mM Bacillus subtilis
GDP 64% inhibition at 5 mM Bacillus subtilis
GMP 88% inhibition at 5 mM Bacillus subtilis
L-histidine no inhibition Bacillus subtilis
L-tryptophan no inhibition Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.48
-
 D-ribose 5-phosphate pH 8.2, 37ºC Bacillus subtilis
0.66
-
 ATP pH 8.2, 37ºC Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bacillus subtilis
Mg2+ required to form a complex with ATP and as a free cation Bacillus subtilis
Mg2+ the most effective Bacillus subtilis
Mn2+ can partially replace Mg2+ Bacillus subtilis
Mn2+ 25-30% of the activity with Mg2+ Bacillus subtilis
additional information absolute requirement for a divalent cation for activity Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 8 * 34000, SDS-PAGE Bacillus subtilis
280000
-
 gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-ribose 5-phosphate Bacillus subtilis the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
streptomycin-heat treatment, ammonium sulfate fractionation, chromatography on DEAE-Sepharose and affinity chromatography Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate sequential kinetic mechanism Bacillus subtilis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
190
-
 30fold to 50fold more activity in the cloned enzyme than in the enzyme from the wild-type cells Bacillus subtilis

Storage Stability

Storage Stability Organism
-70ºC, glycerol 10%, stable Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-ribose 5-phosphate
-
 Bacillus subtilis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
ATP + D-ribose 5-phosphate the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan Bacillus subtilis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r

Subunits

Subunits Comment Organism
octamer 8 * 34000, SDS-PAGE Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
7 9.5 at pH 7 and pH 9.5, about 35% and 85% of the maximal activity, respectively Bacillus subtilis