Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NaHCO3 | RuBisCO is activated in the presence of 40 mM NaHCO3 | Rhodospirillum rubrum |
Protein Variants | Comment | Organism |
---|---|---|
K122E | the mutant is almost inactive (0.8% activity compared to the wild type enzyme) | Rhodospirillum rubrum |
K122M | the mutant is almost inactive (0.2% activity compared to the wild type enzyme) | Rhodospirillum rubrum |
K122R | the mutant with 69% activity compared to the wild type enzyme has a 40% decrease in kcat for carboxylase activity, a 2fold increase in Km for CO2, and a 1.9fold increase in Km for D-ribulose 1,5-bisphosphate | Rhodospirillum rubrum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.03 | - |
D-ribulose 1,5-bisphosphate | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
0.0567 | - |
D-ribulose 1,5-bisphosphate | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
0.128 | - |
CO2 | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
0.256 | - |
CO2 | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodospirillum rubrum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
His-bind resin column chromatography | Rhodospirillum rubrum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-ribulose 1,5-bisphosphate + CO2 + H2O | - |
Rhodospirillum rubrum | 3-phospho-D-glycerate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribulose-1,5-bisphosphate carboxylase/oxygenase | - |
Rhodospirillum rubrum |
Rubisco | - |
Rhodospirillum rubrum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
CO2 | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
3 | - |
D-ribulose 1,5-bisphosphate | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
5 | - |
CO2 | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
5 | - |
D-ribulose 1,5-bisphosphate | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
12 | - |
CO2 | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
39 | - |
CO2 | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
54 | - |
D-ribulose 1,5-bisphosphate | mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum | |
160 | - |
D-ribulose 1,5-bisphosphate | wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C | Rhodospirillum rubrum |