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Literature summary for 4.1.1.39 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis O93627
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-ribulose 1,5-bisphosphate + CO2 + H2O
-
Thermococcus kodakarensis 3-phospho-D-glycerate
-
?

Subunits

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

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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