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 (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus subtilis |
General Stability | Organism |
---|---|
relatively stable in absence of phosphate | Bacillus subtilis |
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 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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
34000 | - |
8 * 34000, SDS-PAGE | Bacillus subtilis |
280000 | - |
gel filtration | Bacillus subtilis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
streptomycin-heat treatment, ammonium sulfate fractionation, chromatography on DEAE-Sepharose and affinity chromatography | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate | sequential kinetic mechanism | Bacillus subtilis |
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 | Organism |
---|---|
-70ºC, glycerol 10%, stable | Bacillus subtilis |
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 | Comment | Organism |
---|---|---|
octamer | 8 * 34000, SDS-PAGE | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 8.5 | - |
Bacillus subtilis |
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 |