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Literature summary for 4.1.1.39 extracted from

  • Marcus, Y.; Altman-Gueta, H.; Finkler, A.; Gurevitz, M.
    Mutagenesis at two distinct phosphate-binding sites unravels their differential roles in regulation of Rubisco activation and catalysis (2005), J. Bacteriol., 187, 4222-4228.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H310A turnover number for D-ribulose 1,5-bisphosphate is nearly identical to wild-type value, 1.3fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.
H310D 2.9fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 2.8fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.
H327Q 5.9fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 3.5fold increase in KM-value for D-ribulose 1,5-bisphosphate, 8.7fold decrease in Ki-value for phosphate Synechocystis sp.
H398A 12.7fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 1.9fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.
K305A 3.1fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 1.4fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.
K305E 2.9fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 1.7fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.
R134A 3.1fold decrease in turnover number for D-ribulose 1,5-bisphosphate, 1.5fold increase in KM-value for D-ribulose 1,5-bisphosphate Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
D-ribulose 1,5-bisphosphate wild-type enzyme Synechocystis sp.
0.161
-
CO2 mutant enzyme R134A Synechocystis sp.
0.179
-
D-ribulose 1,5-bisphosphate mutant enzyme H310A Synechocystis sp.
0.181
-
CO2 wild-type enzyme Synechocystis sp.
0.185
-
CO2 mutant enzyme K305A Synechocystis sp.
0.19
-
CO2 mutant enzyme K305E Synechocystis sp.
0.199
-
D-ribulose 1,5-bisphosphate mutant enzyme K305A Synechocystis sp.
0.212
-
D-ribulose 1,5-bisphosphate mutant enzyme R134A Synechocystis sp.
0.242
-
D-ribulose 1,5-bisphosphate mutant enzyme K305E Synechocystis sp.
0.267
-
D-ribulose 1,5-bisphosphate mutant enzyme H298A Synechocystis sp.
0.387
-
D-ribulose 1,5-bisphosphate mutant enzyme H310D Synechocystis sp.
0.49
-
D-ribulose 1,5-bisphosphate mutant enzyme H327Q Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
strain PCC 6803
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.72
-
D-ribulose 1,5-bisphosphate mutant enzyme H298A Synechocystis sp.
1.53
-
D-ribulose 1,5-bisphosphate mutant enzyme H327Q Synechocystis sp.
2.95
-
D-ribulose 1,5-bisphosphate mutant enzyme K305A Synechocystis sp.
2.97
-
D-ribulose 1,5-bisphosphate mutant enzyme R134A Synechocystis sp.
3.08
-
D-ribulose 1,5-bisphosphate mutant enzyme H310D Synechocystis sp.
3.08
-
D-ribulose 1,5-bisphosphate mutant enzyme K305E Synechocystis sp.
9
-
D-ribulose 1,5-bisphosphate mutant enzyme H310A Synechocystis sp.
9.08
-
D-ribulose 1,5-bisphosphate wild-type enzyme Synechocystis sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.67
-
phosphate mutant enzyme H327Q Synechocystis sp.
5.7
-
phosphate mutant enzyme K305E Synechocystis sp.
5.8
-
phosphate wild-type enzyme Synechocystis sp.
6
-
phosphate mutant enzyme R134A Synechocystis sp.
6.3
-
phosphate mutant enzyme H298A Synechocystis sp.