Information on EC 5.3.1.34 - D-erythrulose 4-phosphate isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
5.3.1.34
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RECOMMENDED NAME
GeneOntology No.
D-erythrulose 4-phosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-erythrulose 4-phosphate = D-erythrose 4-phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-threitol degradation
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erythritol degradation I
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erythritol degradation II
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L-threitol degradation
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SYSTEMATIC NAME
IUBMB Comments
D-erythrulose-4-phosphate ketose-aldose isomerase
The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate
D-erythrulose 4-phosphate
show the reaction diagram
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initially D-threose 4-phosphate is also formed. After 240 min, about 90% of tetrose 4-phosphate is D-erythrulose 4-phosphate, 5% is D-threose 4-phosphate
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?
D-erythrulose 4-phosphate
D-erythrose 4-phosphate
show the reaction diagram
D-ribulose-5-phosphate
D-xylulose 5-phosphate
show the reaction diagram
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strong D-ribulose-5-phosphate 3-epimerase activity, reaction of EC 5.1.3.1
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?
D-threose 4-phosphate
D-erythrulose 4-phosphate
show the reaction diagram
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130% of the activity with D-erythrose 4-phosphate
D-threose 4-phosphate isomerizes non-enzymatically more easily than D-erythrose 4-phosphate to D-erythrulose 4-phosphate
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?
additional information
?
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enzyme can catalyze simultaneously both the isomerization and epimerization of D-erythrose 4-phosphate to D-erythrulose 4-phosphate and D-threose 4-phosphate. No isomerase activity with D-glyceraldehyde 3-phosphate, D-ribose 5-phosphate, D-glucose 6-phosphate and D-fructose 6-phosphate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-erythrulose 4-phosphate
D-erythrose 4-phosphate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
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0.1 mM, 100% inhibition of D-erythrose 4-phosphate isomerase activity
pentulose 5-phosphate
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i.e. enzymatic equilibrium mixture of D-ribulose 5-phosphate and D-xylulose 5-phosphate, 1 mM, 63% inhibition
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potassium phosphate
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10 mM, 45% inhibition of D-erythrose 4-phosphate isomerase activity
Sodium sulfate
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20 mM, 66% inhibition of D-erythrose 4-phosphate isomerase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.05
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substrate D-erythrose 4-phosphate, pH 7.0, 30°C
6570
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substrate D-ribulose-5-phosphate, pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 22500, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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22 h, 0°C, stable
738147
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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10 min, stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Bistris/HCl buffer (pH 7.0), stable for about six months without any loss of enzymatic activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
rpiB is inserted into a pET15b vector, which allows expression of N-terminal His-tagged proteins in Escherichia coli Bl21pLysS
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