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Literature summary extracted from

  • Johnson, A.E.; Tanner, M.E.
    Epimerization via carbon - carbon bond cleavage. L-Ribulose-5-phosphate 4-epimerase as a masked class II aldolase (1998), Biochemistry, 37, 5746-5754.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.4 overexpression Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
5.1.3.4 D76N site-directed mutants in which the putative metal ion ligand is modified: H95N, H97N, D76N. The mutant enzymes require exogenous metal ions for full activity. Their turnover numbers are greatly reduced whereas the Km-values are only moderately affected. Low levels of aldolase activity are observed with the H97N mutant, but not with D76N or the H95N mutants. The H97N mutant enzyme catalyzes the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose 5-phosphate and D-xylulose 5-phosphate Escherichia coli
5.1.3.4 D76N the ratio of turnover number to Km-value is 348fold lower than that of the wild-type enzyme Escherichia coli
5.1.3.4 H59N site-directed mutants in which the putative metal ion ligand is modified: H95N, H97N, D76N. The mutant enzymes require exogenous metal ions for full activity. Their turnover numbers are greatly reduced whereas the Km-values are only moderately affected. Low levels of aldolase activity are observed with the H97N mutant, but not with D76N or the H95N mutants. The H97N mutant enzyme catalyzes the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose 5-phosphate and D-xylulose 5-phosphate Escherichia coli
5.1.3.4 H95N the ratio of turnover number to Km-value is 676fold lower than that of the wild-type enzyme Escherichia coli
5.1.3.4 H97N site-directed mutants in which the putative metal ion ligand is modified: H95N, H97N, D76N. The mutant enzymes require exogenous metal ions for full activity. Their turnover numbers are greatly reduced whereas the Km-values are only moderately affected. Low levels of aldolase activity are observed with the H97N mutant, but not with D76N or the H95N mutants. The H97N mutant enzyme catalyzes the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose 5-phosphate and D-xylulose 5-phosphate Escherichia coli
5.1.3.4 H97N mutant enzyme with low levels of aldolase activity. The ratio of turnover number to Km-value is 479fold lower than that of the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.4 glycoaldehyde phosphate competitive inhibitor of mutant enzyme H97N but not of the wild-type enzyme Escherichia coli
5.1.3.4 glycolaldehyde
-
 Escherichia coli
5.1.3.4 glycolaldehyde phosphate competitive inhibition of H97N mutant enzyme, no inhibition of wild type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.4 0.06
-
 L-ribulose 5-phosphate wild type enzyme, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 0.06
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, wild-type enzyme Escherichia coli
5.1.3.4 0.087
-
 L-ribulose 5-phosphate wild type enzyme, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.087
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, wild-type Escherichia coli
5.1.3.4 0.096
-
 L-ribulose 5-phosphate mutant H95N, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 0.096
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H95N Escherichia coli
5.1.3.4 0.1
-
 L-ribulose 5-phosphate L-ribulose 5-phosphate, mutant H97N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.1
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H95N Escherichia coli
5.1.3.4 0.11
-
 L-ribulose 5-phosphate mutant D76N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.11
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme D76N Escherichia coli
5.1.3.4 0.14
-
 L-ribulose 5-phosphate L-ribulose 5-phosphate, mutant H97N and D76N, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 0.14
-
 L-ribulose 5-phosphate mutant H95N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.14
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N or D76N Escherichia coli
5.1.3.4 0.14
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H97N Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.4 Cu2+ the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+ Escherichia coli
5.1.3.4 Mn2+ the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+ Escherichia coli
5.1.3.4 Zn2+ H95N, H97N, and D76N mutant enzymes require exogenous metal ions for full activity Escherichia coli
5.1.3.4 Zn2+ the enzyme preparation contains a mixture of the following metals in order of decreasing abundance: Zn2+, Mn2+, Cu2+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.3.4 25522
-
 4 * 25522, electrospray mass spectrometry Escherichia coli
5.1.3.4 127000
-
 wild-type enzyme and mutant enzymes H97N, D76N and H95N, gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.4 Escherichia coli
-
-
-
5.1.3.4 Escherichia coli
-
 wild type enzyme and mutants H95N, H97N, and D76N
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.4
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.3.4 34
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.4 L-Ribulose 5-phosphate
-
 Escherichia coli D-Xylulose 5-phosphate
-
 ?
5.1.3.4 additional information the mutant enzyme H97N catalyzes the condensation of dihydroxyacetone and glycolaldehyde to produce a mixture of ribulose-5-phosphate and D-xylulose 5-phosphate Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.3.4 tetramer 4 * 25522, electrospray mass spectrometry Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.4 50 55 thermal denaturation themperature of wild-type enzyme and mutant enzymes H97N, D76N and H95N Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.4 0.047
-
 L-ribulose 5-phosphate mutant H95N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.047
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H95N Escherichia coli
5.1.3.4 0.048
-
 L-ribulose 5-phosphate mutant H97N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.048
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H97N Escherichia coli
5.1.3.4 0.073
-
 L-ribulose 5-phosphate mutant D76N, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 0.073
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme D76N Escherichia coli
5.1.3.4 0.1
-
 L-ribulose 5-phosphate mutant H95N, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 0.16
-
 L-ribulose 5-phosphate mutant D76N, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 0.16
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme D76N Escherichia coli
5.1.3.4 7.3
-
 L-ribulose 5-phosphate mutant H97N, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 7.3
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N Escherichia coli
5.1.3.4 20.4
-
 L-ribulose 5-phosphate wild type enzyme, Zn2+ form of enzyme after dialysis Escherichia coli
5.1.3.4 20.4
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis, wild-type Escherichia coli
5.1.3.4 20.7
-
 L-ribulose 5-phosphate wild type enzyme, Zn2+ form of enzyme plus 0.1 mM Zn2+ Escherichia coli
5.1.3.4 22.4
-
 L-ribulose 5-phosphate 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, wild-type enzyme Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.3.4 0.37
-
 glycolaldehyde 37°C, pH 7.6, mutant enzyme H97N, with L-ribulose 5-phosphate as substrate Escherichia coli