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Literature summary for 1.1.1.267 extracted from

  • Fernandes, R.P.; Proteau, P.J.
    Kinetic characterization of Synechocystis sp. PCC6803 1-deoxy-D-xylulose 5-phosphate reductoisomerase mutants (2006), Biochim. Biophys. Acta, 1764, 223-229.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
D152A site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.1% activity compared to the wild-type enzyme Synechocystis sp.
D152N site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant Synechocystis sp.
E154D site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.28% activity compared to the wild-type enzyme Synechocystis sp.
E154Q site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.008% activity compared to the wild-type enzyme Synechocystis sp.
E223H site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.007% activity compared to the wild-type enzyme Synechocystis sp.
E223Q site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant Synechocystis sp.
H155A site-directed mutagenesis, active site mutant, in sense and antisense orientation, 32% activity compared to the wild-type enzyme Synechocystis sp.
M206A site-directed mutagenesis, active site mutant, in sense and antisense orientation, 9% activity compared to the wild-type enzyme Synechocystis sp.
M206V site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant Synechocystis sp.
S153A site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.11% activity compared to the wild-type enzyme Synechocystis sp.
S153N site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.76% activity compared to the wild-type enzyme Synechocystis sp.
S153T site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.8% activity compared to the wild-type enzyme Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
fosmidomycin
-
Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics, recombinant His-tagged wild-type and mutant enzymes Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required for activity Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-deoxy-D-xylulose 5-phosphate + NADPH + H+ Synechocystis sp. second step of the methylerythritol 4-phosphate pathway 2-C-methyl-D-erythritol 4-phosphate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
strain PCC6803
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by metal ion affinity chromatography Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
-
Synechocystis sp. 2-C-methyl-D-erythritol 4-phosphate + NADP+
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+ second step of the methylerythritol 4-phosphate pathway Synechocystis sp. 2-C-methyl-D-erythritol 4-phosphate + NADP+
-
?

Synonyms

Synonyms Comment Organism
1-deoxy-D-xylulose 5-phosphate reductoisomerase
-
Synechocystis sp.
DXR
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Synechocystis sp.