Protein Variants | Comment | Organism |
---|---|---|
I312A | mutant retains 30% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
I312A/S363I | mutant retains 75% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
I312S | mutant retains 16% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
I312S/S363I | mutant retains 78% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
I312T | mutant retains 15% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
M295D | mutant retains significantly more activity than the wild-type enzyme when incubated with concentrations of oxygen ranging from 10% to 100% in the gas phase. Mutant shows expected competitive inhibition by O2 with respect to CO2 | Archaeoglobus fulgidus |
M295D/I312A | mutant retains 40% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
M295D/I312A/S363I | mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins | Archaeoglobus fulgidus |
M295D/I312A/S363V | mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins | Archaeoglobus fulgidus |
M295D/I312S | mutant retains 46% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
M295D/I312S/S363I | mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins | Archaeoglobus fulgidus |
M295D/I312S/S363V | mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins | Archaeoglobus fulgidus |
M295D/I312T | mutant retains 45% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions | Archaeoglobus fulgidus |
M295D/S363I | mutant retains significantly more activity than the wild-type enzyme when incubated with concentrations of oxygen ranging from 10% to 100% in the gas phase. Mutant shows expected competitive inhibition by O2 with respect to CO2. The Km value for D-ribulose 1,5-bisphosphate are significantly higher than for the wild-type enzyme | Archaeoglobus fulgidus |
M295D/S363I | significant loss of activity, mutant retains 75% carboxylase activity under oxygen exposed conditions | Thermococcus kodakarensis |
M295D/S363V | mutant retains significantly more activity than the wild-type enzyme when incubated with concentrations of oxygen ranging from 10% to 100% in the gas phase. Mutant shows expected competitive inhibition by O2 with respect to CO2. The Km value for D-ribulose 1,5-bisphosphate are significantly higher than for the wild-type enzyme | Archaeoglobus fulgidus |
M295D/S363V | significant loss of activity, mutant retains 75% carboxylase activity under oxygen exposed conditions | Thermococcus kodakarensis |
M298D | mutant retains 51% carboxylase activity under oxygen exposed conditions | Thermococcus kodakarensis |
S363I | mutant retains significantly more activity than the wild-type enzyme when incubated with concentrations of oxygen ranging from 10% to 100% in the gas phase. Mutant shows expected competitive inhibition by O2 with respect to CO2. The Km value for D-ribulose 1,5-bisphosphate are significantly higher than for the wild-type enzyme | Archaeoglobus fulgidus |
S363V | mutant retains 71% carboxylase activity under oxygen exposed conditions | Thermococcus kodakarensis |
S363V | mutant retains significantly more activity than the wild-type enzyme when incubated with concentrations of oxygen ranging from 10% to 100% in the gas phase. Mutant shows expected competitive inhibition by O2 with respect to CO2. The Km value for D-ribulose 1,5-bisphosphate are significantly higher than for the wild-type enzyme | Archaeoglobus fulgidus |
S366I | mutant retains 75% carboxylase activity under oxygen exposed conditions | Thermococcus kodakarensis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
O2 | wild-type retains 37% activity when exposed to oxygen | Thermococcus kodakarensis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.014 | - |
D-ribulose 1,5-bisphosphate | wild-type, pH 8.3, 83°C | Thermococcus kodakarensis | |
0.02 | - |
D-ribulose 1,5-bisphosphate | wild-type, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.021 | - |
D-ribulose 1,5-bisphosphate | mutant M295D, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.051 | - |
CO2 | wild-type, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.058 | - |
CO2 | mutant M295D, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.062 | - |
CO2 | mutant M295D/S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.074 | - |
CO2 | mutant M295D/S363I, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.079 | - |
CO2 | mutant S363I, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.079 | - |
CO2 | wild-type, pH 8.3, 83°C | Thermococcus kodakarensis | |
0.088 | - |
CO2 | mutant S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.118 | - |
D-ribulose 1,5-bisphosphate | mutant S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
0.57 | - |
D-ribulose 1,5-bisphosphate | mutant S363I, pH 8.3, 83°C | Archaeoglobus fulgidus | |
1.381 | - |
D-ribulose 1,5-bisphosphate | mutant M295D/S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
1.646 | - |
D-ribulose 1,5-bisphosphate | mutant M295D/S363I, pH 8.3, 83°C | Archaeoglobus fulgidus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O28635 | - |
- |
Thermococcus kodakarensis | O93627 | - |
- |
Thermococcus kodakarensis ATCC BAA-918 | O93627 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-ribulose 1,5-bisphosphate + CO2 + H2O | - |
Thermococcus kodakarensis | 2 3-phospho-D-glycerate + 2 H+ | - |
? | |
D-ribulose 1,5-bisphosphate + CO2 + H2O | - |
Archaeoglobus fulgidus | 2 3-phospho-D-glycerate + 2 H+ | - |
? | |
D-ribulose 1,5-bisphosphate + CO2 + H2O | - |
Thermococcus kodakarensis ATCC BAA-918 | 2 3-phospho-D-glycerate + 2 H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AF_1638 | - |
Archaeoglobus fulgidus |
rbcL | - |
Thermococcus kodakarensis |
rbcL | - |
Archaeoglobus fulgidus |
TK2290 | - |
Thermococcus kodakarensis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.7 | - |
D-ribulose 1,5-bisphosphate | mutant M295D/S363I, pH 8.3, 83°C | Archaeoglobus fulgidus | |
4.3 | - |
D-ribulose 1,5-bisphosphate | mutant M295D/S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
9.5 | - |
D-ribulose 1,5-bisphosphate | mutant S363I, pH 8.3, 83°C | Archaeoglobus fulgidus | |
12.4 | - |
D-ribulose 1,5-bisphosphate | mutant S363V, pH 8.3, 83°C | Archaeoglobus fulgidus | |
16.6 | - |
D-ribulose 1,5-bisphosphate | wild-type, pH 8.3, 83°C | Thermococcus kodakarensis | |
17.7 | - |
D-ribulose 1,5-bisphosphate | mutant M295D, pH 8.3, 83°C | Archaeoglobus fulgidus | |
23.1 | - |
D-ribulose 1,5-bisphosphate | wild-type, pH 8.3, 83°C | Archaeoglobus fulgidus |
General Information | Comment | Organism |
---|---|---|
physiological function | Archaeoglobus fulgidus rbcL2 gene product can complement growth under anaerobic photoheterotrophic conditions when expressed in Rhodobacter capsulatus strain SB I/II- | Archaeoglobus fulgidus |