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Literature summary for 4.1.1.39 extracted from

  • Kreel, N.E.; Tabita, F.R.
    Serine 363 of a hydrophobic region of archaeal ribulose 1,5-bisphosphate carboxylase/oxygenase from Archaeoglobus fulgidus and Thermococcus kodakaraensis affects CO2/O2 substrate specificity and oxygen sensitivity (2015), PLoS One, 10, e0138351.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Inhibitors Comment Organism Structure
O2 wild-type retains 37% activity when exposed to oxygen Thermococcus kodakarensis

KM Value [mM]

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

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O28635
-
-
Thermococcus kodakarensis O93627
-
-
Thermococcus kodakarensis ATCC BAA-918 O93627
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
AF_1638
-
Archaeoglobus fulgidus
rbcL
-
Thermococcus kodakarensis
rbcL
-
Archaeoglobus fulgidus
TK2290
-
Thermococcus kodakarensis

Turnover Number [1/s]

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

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