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Information on EC 5.1.3.1 - ribulose-phosphate 3-epimerase and Organism(s) Spinacia oleracea and UniProt Accession Q43157

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.1 ribulose-phosphate 3-epimerase
IUBMB Comments
The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
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This record set is specific for:
Spinacia oleracea
UNIPROT: Q43157
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The taxonomic range for the selected organisms is: Spinacia oleracea
The enzyme appears in selected viruses and cellular organisms
Synonyms
rpe, d-ribulose-5-phosphate 3-epimerase, ribulose 5-phosphate 3-epimerase, ribulose-5-phosphate 3-epimerase, ribulose-phosphate 3-epimerase, d-ribulose 5-phosphate 3-epimerase, pentose-5-phosphate 3-epimerase, r5p3e, cyt-rpease, rpease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Ribulose phosphate-3-epimerase
-
-
-
-
D-Ribulose-5-P 3-epimerase
-
-
-
-
D-Ribulose-5-phosphate epimerase
-
-
-
-
D-Xylulose-5-phosphate 3-epimerase
-
-
-
-
Epimerase, ribulose phosphate 3-
-
-
-
-
Pentose-5-phosphate 3-epimerase
-
-
-
-
Phosphoketopentose 3-epimerase
-
-
-
-
Phosphoketopentose epimerase
-
-
-
-
Phosphoribulose epimerase
-
-
-
-
PPE
-
-
-
-
R5P3E
-
-
-
-
Ribulose 5-phosphate 3-epimerase
-
-
-
-
Ribulose phosphate 3-epimerase
-
-
-
-
RPE
-
-
-
-
Xylulose phosphate 3-epimerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-ribulose-5-phosphate 3-epimerase
The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-20-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
additional information
?
-
-
enzyme is integral to both the Calvin cycle and the oxidative pentose phosphate pathway
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is integral to both the Calvin cycle and the oxidative pentose phosphate pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DL-alpha-glycerophosphate
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 2.1
D-ribulose 5-phosphate
0.25
D-ribulose 5-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00033 - 7100
D-ribulose 5-phosphate
0.138
D-ribulose 5-phosphate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
DL-alpha-glycerophosphate
25°C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
-
reaction with D-ribulose 5-phosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: about 90% of maximal activity, pH 9.0: 95% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 6.8
wild-type enzyme and mutant enzyme D186E, denaturing isoelectric focusing, pH gradient 5-8
6.6
mutant enzymes D186A and D186N, denaturing isoelectric focusing, pH gradient 5-8
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPE_SPIOL
285
0
30366
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
25000
8 * 25000, SDS-PAGE
180000
-
gel filtration
23000
-
8 * 23000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 25000, SDS-PAGE
octamer
-
8 * 23000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D186A
KM-value for D-ribulose 5-phosphate is increased 10fold, turnover-number is decreased to less than 0.1% of the wild-type value
D186E
KM-value for D-ribulose 5-phosphate is unaltered, turnover-number is decreased to less than 0.1% of the wild-type value
D186N
KM-value for D-ribulose 5-phosphate is unaltered, turnover-number is decreased to less than 0.1% of the wild-type value
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DL-alpha-glycerophosphate or ethanol stabilize the extremely labile recombinant enzyme, but are unable to reverse the spontaneous loss of activity
drastically destabilized by 2-mercaptoethanol
DTT destabilizes
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, wether in crude extracts or highly purified, the recombinant enzyme is inherently unstable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes D186A, D186N, D186E
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nowitzki, U.; Wyrich, R.; Westhoff, P.; Henze, K.; Scharrenberger, C.; Martin, W.
Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects
Plant Mol. Biol.
29
1279-1291
1995
Spinacia oleracea
Manually annotated by BRENDA team
Teige, M.; Melzer, M.; Suss, K.H.
Purification, properties and in situ localization of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts
Eur. J. Biochem.
252
237-244
1989
Spinacia oleracea
Manually annotated by BRENDA team
Chen, Y.R.; Larimer, F.W.; Serpersu, E.H.; Hartman, F.C.
Identification of a catalytic aspartyl residue of D-ribulose 5-phosphate 3-epimerase by site-directed mutagenesis
J. Biol. Chem.
274
2132-2136
1999
Spinacia oleracea (Q43157), Spinacia oleracea
Manually annotated by BRENDA team
Chen, Y.R.; Hartman, F.C.; Lu, T.Y.; Larimer, F.W.
D-Ribulose-5-phosphate 3-epimerase: cloning and heterologous expression of the spinach gene, and purification and characterization of the recombinant enzyme
Plant Physiol.
118
199-207
1998
Spinacia oleracea (Q43157), Spinacia oleracea
Manually annotated by BRENDA team