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Literature summary for 4.1.1.39 extracted from

  • Nakano, T.; Ashida, H.; Mizohata, E.; Matsumura, H.; Yokota, A.
    An evolutionally conserved Lys122 is essential for function in Rhodospirillum rubrum bona fide RuBisCO and Bacillus subtilis RuBisCO-like protein (2010), Biochem. Biophys. Res. Commun., 392, 212-216.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
NaHCO3 RuBisCO is activated in the presence of 40 mM NaHCO3 Rhodospirillum rubrum

Protein Variants

Protein Variants Comment Organism
K122E the mutant is almost inactive (0.8% activity compared to the wild type enzyme) Rhodospirillum rubrum
K122M the mutant is almost inactive (0.2% activity compared to the wild type enzyme) Rhodospirillum rubrum
K122R the mutant with 69% activity compared to the wild type enzyme has a 40% decrease in kcat for carboxylase activity, a 2fold increase in Km for CO2, and a 1.9fold increase in Km for D-ribulose 1,5-bisphosphate Rhodospirillum rubrum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
D-ribulose 1,5-bisphosphate wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
0.0567
-
D-ribulose 1,5-bisphosphate mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
0.128
-
CO2 wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
0.256
-
CO2 mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His-bind resin column chromatography Rhodospirillum rubrum

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ribulose-1,5-bisphosphate carboxylase/oxygenase
-
Rhodospirillum rubrum
Rubisco
-
Rhodospirillum rubrum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3
-
CO2 mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
3
-
D-ribulose 1,5-bisphosphate mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
5
-
CO2 wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
5
-
D-ribulose 1,5-bisphosphate wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12
-
CO2 mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
39
-
CO2 wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
54
-
D-ribulose 1,5-bisphosphate mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum
160
-
D-ribulose 1,5-bisphosphate wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C Rhodospirillum rubrum