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Literature summary extracted from

  • Nishitani, Y.; Yoshida, S.; Fujihashi, M.; Kitagawa, K.; Doi, T.; Atomi, H.; Imanaka, T.; Miki, K.
    Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile (2010), J. Biol. Chem., 285, 39339-39347.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.39 expressed in Escherichia coli BL21(DE3)CodonPlus RIL cells and Rosetta2(DE3)pLysS cells Thermococcus kodakarensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.39 hanging drop vapor diffusion method, using 100 mM acetate buffer (pH 6.0), 80-100 mM CaCl2, 5-6% (w/v) polyethylene glycol 6,000, and 10% (v/v) 2-methylpentane-2,4-diol Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.39 V330T the mutant shows increased activity and reduced thermal stability compared to the wild type enzyme Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.39 2-carboxy-D-arabinitol 1,5-bisphosphate
-
 Thermococcus kodakarensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.39 0.06
-
 CO2 wild type enzyme, in 100 mM Bicine-NaOH (pH 8.3) and 10 mM MgCl2, temperature not specified in the publication Thermococcus kodakarensis
4.1.1.39 0.067
-
 CO2 mutant enzyme V330T, in 100 mM Bicine-NaOH (pH 8.3) and 10 mM MgCl2, temperature not specified in the publication Thermococcus kodakarensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.39 Mg2+ the active site contains a Mg2+ ion Thermococcus kodakarensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.39 50000
-
 x * 50000, estimated from amino acid sequence Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.39 Thermococcus kodakarensis O93627
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.39 anion exchange column chromatography and Superdex 200 gel filtration Thermococcus kodakarensis

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 3-phospho-D-glycerate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.39 ? x * 50000, estimated from amino acid sequence Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.39 ribulose-1,5-bisphosphate carboxylase/oxygenase
-
 Thermococcus kodakarensis
4.1.1.39 type III Rubisco
-
 Thermococcus kodakarensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.39 90 100 the wild type enzyme shows half-lives of 220 min at 90°C and 48 min at 100°C 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 0.31
-
 CO2 wild type enzyme, in 100 mM Bicine-NaOH (pH 8.3) and 10 mM MgCl2, temperature not specified in the publication Thermococcus kodakarensis
4.1.1.39 0.53
-
 CO2 mutant enzyme V330T, in 100 mM Bicine-NaOH (pH 8.3) and 10 mM MgCl2, temperature not specified in the publication Thermococcus kodakarensis