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Literature summary for 2.7.6.1 extracted from
- Pcal_1127, a highly stable and efficient ribose-5-phosphate pyrophosphokinase from Pyrobaculum calidifontis (2016), Extremophiles, 20, 821-830.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Pcal_1127, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Pyrobaculum calidifontis |
General Stability
| General Stability | Organism |
|---|---|
| Pcal_1127 is stable against denaturants, the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride | Pyrobaculum calidifontis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Pyrobaculum calidifontis |  |
| additional information | the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride | Pyrobaculum calidifontis | |
| phosphate | - |
Pyrobaculum calidifontis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.06 | - |
D-ribose 5-phosphate | pH 10.5, 55°C, recombinant enzyme | Pyrobaculum calidifontis | |
| 0.08 | - |
ATP | pH 10.5, 55°C, recombinant enzyme | Pyrobaculum calidifontis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Pyrobaculum calidifontis | |
| Cd2+ | activates | Pyrobaculum calidifontis | |
| Co2+ | activates | Pyrobaculum calidifontis | |
| Cu2+ | activates | Pyrobaculum calidifontis | |
| Hg2+ | activates | Pyrobaculum calidifontis | |
| Mg2+ | required, highly activating | Pyrobaculum calidifontis | |
| Mn2+ | activates, best stimulating divalent metal ion | Pyrobaculum calidifontis | |
| Ni2+ | activates | Pyrobaculum calidifontis | |
| Zn2+ | activates, highly activating | Pyrobaculum calidifontis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32000 | - |
recombinant enzyme, gel filtration | Pyrobaculum calidifontis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-ribose 5-phosphate | Pyrobaculum calidifontis | - |
AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| ATP + D-ribose 5-phosphate | Pyrobaculum calidifontis JCM 11548 | - |
AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrobaculum calidifontis | A3MV85 | gene Pcal_1127 | - |
| Pyrobaculum calidifontis JCM 11548 | A3MV85 | gene Pcal_1127 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme 4.6fold from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment at 80°C for 25 min, anion exchange chromatography, dialysis, and another step of anion exchange chromatography | Pyrobaculum calidifontis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | optimal growth temperature of Pyrobaculum calidifontis is between 90°C and 95°C | Pyrobaculum calidifontis | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 480 | - |
pH 10.5, 55°C, purified recombinant enzyme | Pyrobaculum calidifontis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| ATP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis JCM 11548 | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| CTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis | CMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| CTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis JCM 11548 | CMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| dATP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis | dAMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| dATP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis JCM 11548 | dAMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| GTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis | GMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| GTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis JCM 11548 | GMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| UTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis | UMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| UTP + D-ribose 5-phosphate | - |
Pyrobaculum calidifontis JCM 11548 | UMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 32741, sequence calculation and SDS-PAGE | Pyrobaculum calidifontis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pcal_1127 | - |
Pyrobaculum calidifontis |
| ribose-5-phosphate pyrophosphokinase | - |
Pyrobaculum calidifontis |
| RPPK | - |
Pyrobaculum calidifontis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
- |
Pyrobaculum calidifontis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | 100 | Pcal_1127 is thermo-stable, Pcal_1127 exhibits more than 95% residual activity after heating for 4 h at 90°C and a half-life of 15 min in the boiling water | Pyrobaculum calidifontis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 311 | - |
D-ribose 5-phosphate | pH 10.5, 55°C, recombinant enzyme | Pyrobaculum calidifontis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
- |
Pyrobaculum calidifontis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | best cofactor, Pcal_1127 exhibits slightly higher activity with dATP compared to ATP as diphosphate donor | Pyrobaculum calidifontis | |
| CTP | can partially substitute for ATP | Pyrobaculum calidifontis | |
| dATP | best cofactor, Pcal_1127 exhibits slightly higher activity with dATP compared to ATP as diphosphate donor | Pyrobaculum calidifontis | |
| GTP | can partially substitute for ATP | Pyrobaculum calidifontis | |
| UTP | low activity | Pyrobaculum calidifontis | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pyrobaculum calidifontis | sequence calculation | - |
6.97 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | ribose-5-phosphate diphosphokinase catalyzes the transfer of pyrophosphoryl group from ATP to C1 hydroxyl group of ribose-5-phosphate resulting in the production of AMP and phosphoribosyl diphosphate, the latter plays a central role in several processes of life, including the synthesis of nucleotides, co-enzyme NAD+, and amino acids histidine and tryptophan | Pyrobaculum calidifontis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5183 | - |
D-ribose 5-phosphate | pH 10.5, 55°C, recombinant enzyme | Pyrobaculum calidifontis | |
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Release 2023.1 (January 2023)
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