5.1.3.4: L-ribulose-5-phosphate 4-epimerase
This is an abbreviated version!
For detailed information about L-ribulose-5-phosphate 4-epimerase, go to the full flat file.
Word Map on EC 5.1.3.4
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5.1.3.4
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l-fuculose-1-phosphate
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l-arabinose
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epimerization
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l-ribulokinase
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dihydroxyacetone
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arabad
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aldol
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glycolaldehyde
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aldolases
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typhimurium
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sphere
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d-glucose
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flip
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ara
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enolate
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aerogenes
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carbon-carbon
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stereocenter
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aerobacter
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l-rhamnulose-1-phosphate
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aldolase-like
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synthesis
- 5.1.3.4
- l-fuculose-1-phosphate
- l-arabinose
-
epimerization
- l-ribulokinase
- dihydroxyacetone
-
arabad
-
aldol
- glycolaldehyde
- aldolases
- typhimurium
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sphere
- d-glucose
- flip
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ara
-
enolate
- aerogenes
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carbon-carbon
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stereocenter
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aerobacter
- l-rhamnulose-1-phosphate
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aldolase-like
- synthesis
Reaction
Synonyms
araD, Epimerase, L-ribulose phosphate 4-, L-Ribulose phosphate 4-epimerase, L-Ribulose-5-phosphate 4-epimerase, Phosphoribulose isomerase, Ribulose phosphate 4-epimerase
ECTree
5.1.3.4 L-ribulose-5-phosphate 4-epimeraseAdvanced search results
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results (Engineering
Engineering on EC 5.1.3.4 - L-ribulose-5-phosphate 4-epimerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D120N
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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
D76E
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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
D76N
E142Q
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the ratio of turnover number to Km-value is 17fold lower than that of the wild-type enzyme
H218N
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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
H59N
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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
H95N
H97N
K42M
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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
N28A
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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
Y229F
D76N
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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
D76N
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the ratio of turnover number to Km-value is 348fold lower than that of the wild-type enzyme
H95N
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the ratio of turnover number to Km-value is 24.1fold lower than that of the wild-type enzyme when activated with ZnCl2
H95N
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the ratio of turnover number to Km-value is 676fold lower than that of the wild-type enzyme
H97N
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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
H97N
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13C isotope effects at pH 7 are 3.25% at C-3 and 2.69% at C4, compared to 1.85% and 1.5% for the wild-type enzyme
H97N
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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
H97N
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the ratio of turnover number to Km-value is 4011fold lower than that of the wild-type enzyme when activated with ZnCl2
Y229F
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13C isotope effects at pH 7 are 2.53% at C-3 and 1.99% at C4, compared to 1.85% and 1.5% for the wild-type enzyme
Y229F
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the ratio of turnover number to Km-value is 182.5fold lower than that of the wild-type enzyme when activated with ZnCl2
