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Literature summary for 5.1.3.4 extracted from

  • Samuel, J.; Luo, Y.; Morgan, P.M.; Strynadka, N.C.; Tanner, M.E.
    Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase (2001), Biochemistry, 40, 14772-14780.
    View publication on PubMed
Search for more literature for 5.1.3.4

Protein Variants

Protein Variants Comment Organism
D120N 3000fold decrease in the value of turnover number. The structure is indistinguishable from that of the wild-type enzyme and the decrease in activity is not simply due to a strutural perturbation of active site. The ratio of turnover number to Km-value is 20750fold lower than that of the wild-type enzyme Escherichia coli
D76E the ratio of turnover number to Km-value is 104fold lower than that of the wild-type enzyme,2.2fold decrease in backgroud aldolase activity compared to wild-type enzyme Escherichia coli
E142Q the ratio of turnover number to Km-value is 17fold lower than that of the wild-type enzyme Escherichia coli
H218N 15fold decrease in background aldolase activity compared to wild-type enzyme. The ratio of turnover number to Km-value is 296fold lower than that of the wild-type enzyme Escherichia coli
K42M the ratio of turnover number to Km-value is 12969fold lower than that of the wild-type enzyme, 5.3fold increase in backgroud aldolase activity compared to wild-type enzyme Escherichia coli
N28A the ratio of turnover number to Km-value is 198fold lower than that of the wild-type enzyme, 10.2fold increase in backgroud aldolase activity compared to wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.047
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli
0.086
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
0.25
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D76E Escherichia coli
0.28
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D120N Escherichia coli
0.58
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
1.2
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme N28A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes expressed in Escherichia coli Y1090 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
-
 ?
additional information wild-type enzyme and mutant enzymes D76E and N28A display a background aldolase activity with glycolaldehyde, phosphate and dihydroxyacetone Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0057
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D120N Escherichia coli
0.81
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
1
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D76E Escherichia coli
1.1
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli
2.14
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
2.5
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme N28A Escherichia coli
2.94
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
6.08
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
19.4
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli