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Literature summary for 5.1.3.4 extracted from

  • Lee, L.V.; Poyner, R.R.; Vu, M.V.; Cleland, W.W.
    Role of metal ions in the reaction catalyzed by L-ribulose-5-phosphate 4-epimerase (2000), Biochemistry, 39, 4821-4830.
    View publication on PubMed
Search for more literature for 5.1.3.4

Protein Variants

Protein Variants Comment Organism
H95N the ratio of turnover number to Km-value is 24.1fold lower than that of the wild-type enzyme when activated with ZnCl2 Escherichia coli
H97N the ratio of turnover number to Km-value is 4011fold lower than that of the wild-type enzyme when activated with ZnCl2 Escherichia coli
Y229F the ratio of turnover number to Km-value is 182.5fold lower than that of the wild-type enzyme when activated with ZnCl2 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0471
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM ZnCl2 Escherichia coli
0.091
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme H95N, activated by 0.1 mM ZnCl2 Escherichia coli
0.11
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM CoCl2 Escherichia coli
0.129
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme Y229F, activated by 0.1 mM ZnCl2 Escherichia coli
0.132
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme H97N, activated by 0.1 mM ZnCl2 Escherichia coli
0.415
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MnCl2 Escherichia coli
0.493
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MgCl2 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can replace Zn2+ in mutant enzyme Y229F and in wild-type enzyme, Km-value for wild-type enzyme is 0.00029 mM Escherichia coli
Mg2+ poorly bound, weak activator, KM-value for wild-type enzyme is 1.35 mM Escherichia coli
Mn2+ can replace Zn2+ in mutant enzyme Y229F and in wild-type enzyme. Km-value for wild-type enzyme is 0.00054 mM Escherichia coli
additional information His95 and His97 are likely metal ion ligands Escherichia coli
Zn2+ physiological activator, KM-value for wild-type enzyme is 0.00017 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ribulose 5-phosphate
-
 Escherichia coli D-Xylulose 5-phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0118
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme Y229F, activated by 0.1 mM ZnCl2 Escherichia coli
0.183
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme H95N, activated by 0.1 mM ZnCl2 Escherichia coli
0.502
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MgCl2 Escherichia coli
2.01
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme H97N, activated by 0.1 mM ZnCl2 Escherichia coli
2.94
-
 L-ribulose 5-phosphate 22°C, pH 7.5, mutant enzyme H97N, activated by 0.1 mM ZnCl2 Escherichia coli
6.08
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MgCl2 Escherichia coli
17.3
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM ZnCl2 Escherichia coli
21.8
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM CoCl2 Escherichia coli
36.5
-
 L-ribulose 5-phosphate 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MnCl2 Escherichia coli