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Literature summary 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

EC Number Protein Variants Comment Organism
4.1.1.39 I312A mutant retains 30% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 I312A/S363I mutant retains 75% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 I312S mutant retains 16% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 I312S/S363I mutant retains 78% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 I312T mutant retains 15% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 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
4.1.1.39 M295D/I312A mutant retains 40% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 M295D/I312A/S363I mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins Archaeoglobus fulgidus
4.1.1.39 M295D/I312A/S363V mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins Archaeoglobus fulgidus
4.1.1.39 M295D/I312S mutant retains 46% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 M295D/I312S/S363I mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins Archaeoglobus fulgidus
4.1.1.39 M295D/I312S/S363V mutant displays substantially lower levels of activity in comparison to the single as well as double mutant proteins Archaeoglobus fulgidus
4.1.1.39 M295D/I312T mutant retains 45% activity when exposed to oxygen compared to the enzyme assayed under anaerobic conditions Archaeoglobus fulgidus
4.1.1.39 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
4.1.1.39 M295D/S363I significant loss of activity, mutant retains 75% carboxylase activity under oxygen exposed conditions Thermococcus kodakarensis
4.1.1.39 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
4.1.1.39 M295D/S363V significant loss of activity, mutant retains 75% carboxylase activity under oxygen exposed conditions Thermococcus kodakarensis
4.1.1.39 M298D mutant retains 51% carboxylase activity under oxygen exposed conditions Thermococcus kodakarensis
4.1.1.39 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
4.1.1.39 S363V mutant retains 71% carboxylase activity under oxygen exposed conditions Thermococcus kodakarensis
4.1.1.39 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
4.1.1.39 S366I mutant retains 75% carboxylase activity under oxygen exposed conditions Thermococcus kodakarensis

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.39 0.014
-
 D-ribulose 1,5-bisphosphate wild-type, pH 8.3, 83°C Thermococcus kodakarensis
4.1.1.39 0.02
-
 D-ribulose 1,5-bisphosphate wild-type, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.021
-
 D-ribulose 1,5-bisphosphate mutant M295D, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.051
-
 CO2 wild-type, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.058
-
 CO2 mutant M295D, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.062
-
 CO2 mutant M295D/S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.074
-
 CO2 mutant M295D/S363I, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.079
-
 CO2 mutant S363I, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.079
-
 CO2 wild-type, pH 8.3, 83°C Thermococcus kodakarensis
4.1.1.39 0.088
-
 CO2 mutant S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.118
-
 D-ribulose 1,5-bisphosphate mutant S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 0.57
-
 D-ribulose 1,5-bisphosphate mutant S363I, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 1.381
-
 D-ribulose 1,5-bisphosphate mutant M295D/S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 1.646
-
 D-ribulose 1,5-bisphosphate mutant M295D/S363I, pH 8.3, 83°C Archaeoglobus fulgidus

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.39 D-ribulose 1,5-bisphosphate + CO2 + H2O
-
 Thermococcus kodakarensis 2 3-phospho-D-glycerate + 2 H+
-
 ?
4.1.1.39 D-ribulose 1,5-bisphosphate + CO2 + H2O
-
 Archaeoglobus fulgidus 2 3-phospho-D-glycerate + 2 H+
-
 ?
4.1.1.39 D-ribulose 1,5-bisphosphate + CO2 + H2O
-
 Thermococcus kodakarensis ATCC BAA-918 2 3-phospho-D-glycerate + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.39 AF_1638
-
 Archaeoglobus fulgidus
4.1.1.39 rbcL
-
 Thermococcus kodakarensis
4.1.1.39 rbcL
-
 Archaeoglobus fulgidus
4.1.1.39 TK2290
-
 Thermococcus kodakarensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.39 0.7
-
 D-ribulose 1,5-bisphosphate mutant M295D/S363I, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 4.3
-
 D-ribulose 1,5-bisphosphate mutant M295D/S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 9.5
-
 D-ribulose 1,5-bisphosphate mutant S363I, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 12.4
-
 D-ribulose 1,5-bisphosphate mutant S363V, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 16.6
-
 D-ribulose 1,5-bisphosphate wild-type, pH 8.3, 83°C Thermococcus kodakarensis
4.1.1.39 17.7
-
 D-ribulose 1,5-bisphosphate mutant M295D, pH 8.3, 83°C Archaeoglobus fulgidus
4.1.1.39 23.1
-
 D-ribulose 1,5-bisphosphate wild-type, pH 8.3, 83°C Archaeoglobus fulgidus

General Information

EC Number General Information Comment Organism
4.1.1.39 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