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Literature summary for 4.1.1.39 extracted from

  • Alonso, H.; Blayney, M.J.; Beck, J.L.; Whitney, S.M.
    Substrate-induced assembly of Methanococcoides burtonii D-ribulose-1,5-bisphosphate carboxylase/oxygenase dimers into decamers (2009), J. Biol. Chem., 284, 33876-33882.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein and in tobacco chloroplasts Methanococcoides burtonii

Inhibitors

Inhibitors Comment Organism Structure
2-carboxy-D-arabinitol 1,5-bisphosphate
-
Methanococcoides burtonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00013
-
D-ribulose 1,5-bisphosphate pentamer Methanococcoides burtonii
0.13
-
CO2 pentamer Methanococcoides burtonii
2.5
-
O2 pentamer Methanococcoides burtonii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ inhibits activity and promotes pentamer formation Methanococcoides burtonii
Co2+ inhibits activity and promotes pentamer formation Methanococcoides burtonii
Mg2+
-
Methanococcoides burtonii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52857
-
2 * 52857, nondenaturing PAGE analysis, MbR assembles into functional dimers when expressed in Escherichia coli. The catalytic properties of the dimer and the pentamer of MbR are indistinguishable Methanococcoides burtonii
52860
-
monomer, nano ESI-MS Methanococcoides burtonii
105700
-
dimer, nano ESI-MS Methanococcoides burtonii

Organism

Organism UniProt Comment Textmining
Methanococcoides burtonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using metal affinity chromatography Methanococcoides burtonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Ribulose 1,5-bisphosphate + CO2
-
Methanococcoides burtonii ?
-
?
D-ribulose 1,5-bisphosphate + O2
-
Methanococcoides burtonii ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 52857, nondenaturing PAGE analysis, MbR assembles into functional dimers when expressed in Escherichia coli. The catalytic properties of the dimer and the pentamer of MbR are indistinguishable Methanococcoides burtonii
pentamer assembly into pentamers of L2 (L10) occurs when expressed in tobacco chloroplasts or Escherichia coli producing RuBP. In vitro analyses indicate that the sequential assembly of L2 into L10 occurs without chaperone involvement and is stimulated by protein rearrangements associated with either the binding of substrate RuBP, the tight binding transition state analog carboxyarabinitol-1,5-bisphosphate, or inhibitory divalent metal ions within the active site Methanococcoides burtonii

Synonyms

Synonyms Comment Organism
MbR
-
Methanococcoides burtonii
Rubisco
-
Methanococcoides burtonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at, pretreatment at 45°C for 10 min Methanococcoides burtonii
55
-
for both dimer and pentamer Methanococcoides burtonii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.8
-
D-ribulose 1,5-bisphosphate pH 8.0, for both dimer and pentamer Methanococcoides burtonii
4
-
D-ribulose 1,5-bisphosphate pH 6.0, for both dimer and pentamer Methanococcoides burtonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Methanococcoides burtonii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0078
-
2-carboxy-D-arabinitol 1,5-bisphosphate
-
Methanococcoides burtonii