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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.17 cocrystallized with phosphoglycolohydroxamate Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.17 D120N mutant with reduced specific activity Escherichia coli
4.1.2.17 D76E mutant with reduced specific activity Escherichia coli
4.1.2.17 E142Q mutant with increased specific activity Escherichia coli
4.1.2.17 H218N mutant with reduced specific activity Escherichia coli
4.1.2.17 H97N mutant with reduced specific activity Escherichia coli
4.1.2.17 K42M mutant with reduced specific activity, can be inhibited by excess Zn2+ Escherichia coli
4.1.2.17 N28A mutant with reduced specific activity Escherichia coli
5.1.3.4 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
5.1.3.4 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
5.1.3.4 E142Q the ratio of turnover number to Km-value is 17fold lower than that of the wild-type enzyme Escherichia coli
5.1.3.4 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
5.1.3.4 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
5.1.3.4 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.4 0.047
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli
5.1.3.4 0.086
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
5.1.3.4 0.25
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D76E Escherichia coli
5.1.3.4 0.28
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D120N Escherichia coli
5.1.3.4 0.58
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
5.1.3.4 1.2
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme N28A Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.17 Escherichia coli
-
-
-
5.1.3.4 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.4 wild-type and mutant enzymes expressed in Escherichia coli Y1090 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.17 0.00055
-
 H218N mutant Escherichia coli
4.1.2.17 0.0011
-
 D76E mutant Escherichia coli
4.1.2.17 0.0012
-
 D120N mutant Escherichia coli
4.1.2.17 0.0013
-
 K42M mutant Escherichia coli
4.1.2.17 0.0061
-
 N28A mutant Escherichia coli
4.1.2.17 0.0063
-
 H97N mutant Escherichia coli
4.1.2.17 0.0085
-
 wild-type Escherichia coli
4.1.2.17 0.0122
-
 E142Q mutant Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.17 L-fuculose 1-phosphate
-
 Escherichia coli glycerone phosphate + (S)-lactaldehyde
-
 r
5.1.3.4 L-Ribulose 5-phosphate
-
 Escherichia coli D-Xylulose 5-phosphate
-
 ?
5.1.3.4 additional information wild-type enzyme and mutant enzymes D76E and N28A display a background aldolase activity with glycolaldehyde, phosphate and dihydroxyacetone Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.2.17 L-Fuc1P aldolase
-
 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 0.0057
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D120N Escherichia coli
5.1.3.4 0.81
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
5.1.3.4 1
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme D76E Escherichia coli
5.1.3.4 1.1
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli
5.1.3.4 2.14
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
5.1.3.4 2.5
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme N28A Escherichia coli
5.1.3.4 2.94
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme E142Q Escherichia coli
5.1.3.4 6.08
-
 L-ribulose 5-phosphate 37°C, pH 7.6, mutant enzyme H218N Escherichia coli
5.1.3.4 19.4
-
 L-ribulose 5-phosphate 37°C, pH 7.6, wild-type enzyme Escherichia coli