Information on EC 5.1.3.1 - ribulose-phosphate 3-epimerase

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

EC NUMBER
COMMENTARY
5.1.3.1
-
RECOMMENDED NAME
GeneOntology No.
ribulose-phosphate 3-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-ribulose 5-phosphate = D-xylulose 5-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
epimerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
Biosynthesis of secondary metabolites
-
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
formaldehyde assimilation II (RuMP Cycle)
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
heterolactic fermentation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose and glucuronate interconversions
-
Pentose phosphate pathway
-
pentose phosphate pathway (non-oxidative branch)
-
pentose phosphate pathway (partial)
-
Rubisco shunt
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyt-RPEase
Q9SE42
-
D-ribulose 5-phosphate 3-epimerase
Q96AT9
-
D-ribulose 5-phosphate 3-epimerase
-
-
D-ribulose 5-phosphate 3-epimerase
-
-
D-Ribulose phosphate-3-epimerase
-
-
-
-
D-Ribulose-5-P 3-epimerase
-
-
-
-
D-ribulose-5-phosphate 3-epimerase
Q9SE42
-
D-Ribulose-5-phosphate epimerase
-
-
-
-
D-Xylulose-5-phosphate 3-epimerase
-
-
-
-
Epimerase, ribulose phosphate 3-
-
-
-
-
Pentose-5-phosphate 3-epimerase
-
-
-
-
Pentose-5-phosphate 3-epimerase
-
-
Phosphoketopentose 3-epimerase
-
-
-
-
Phosphoketopentose epimerase
-
-
-
-
Phosphoribulose epimerase
-
-
-
-
PPE
-
-
-
-
R5P3E
-
-
-
-
Ribulose 5-phosphate 3-epimerase
-
-
-
-
Ribulose phosphate 3-epimerase
-
-
-
-
ribulose-5-phosphate 3-epimerase
-
-
RPE
-
-
-
-
RPE
Q96AT9
-
RPEase
-
-
Ru5P epimerase
-
-
Ru5P rpimerase
Q43157
-
Ru5Pepimerase
-
-
Xylulose phosphate 3-epimerase
-
-
-
-
xylulose-5-P 3-epimerase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-20-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
mutant strain that lacks D-ribulose-5-phosphate 3-epimerase
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
ox
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
-
-
Manually annotated by BRENDA team
malformed and severely mentally retarded girl with a de novo interstitial deletion 46,XX.del(2)(q32.lq34)
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
construction of strain TMP 3044 with multiple genetic modifications for enhanced xylose growth, one of the modifications is the overexpression of ribulose 5-phosphate epimerase
-
-
Manually annotated by BRENDA team
metabolic engineering of a xylose-isomerase-expressing Saccharomyces cerevisiae strain for rapid anaerobic xylose fermentation. The overexpressed enzymes are EC 2.7.1.17, EC 5.3.1.6, EC 5.3.1.1, EC 2.2.1.1 and EC 2.2.1.2
-
-
Manually annotated by BRENDA team
mutants sensitive to oxidative stress
-
-
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
the growth condition-dependent enzyme is present in the proteomes of wild-type and zwf strains and is downregulated under mixotrophic growth conditions. Twice the amount of xylulose-5-phosphate is synthesized during the Calvin cycle relative to ribose-5-phosphate in mixotrophical growth, and less epimerase is required for maximal conversion of xylulose-5-phosphate to ribulose-5-phosphate, especially during mixotrophic conditions when exogenously added glucose can contribute additional carbon skeletons to the Calvin cycle intermediates
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
r
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
Q43157, -
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
?
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
Pigeon
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
Q9A1H8, -
-
-
-
?
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
-
-
-
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
Q43157, -
-
-
?
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
Q96AT9
-
-
-
r
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
it is proposed that the reaction runs through a cis-ene-diolate intermediate
-
r
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
the reaction mechanism involves a well stabilized cis-enediolate intermediate
-
?
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the Calvin cycle and in the oxidative pentose phosphate pathway
-
r
D-xylulose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
enzyme is involved in carbohydrate metabolism
-
-
-
additional information
?
-
-
enzyme is integral to both the Calvin cycle and the oxidative pentose phosphate pathway
-
-
-
additional information
?
-
-
enzyme of nonoxidative section of the pentose phosphate pathway
-
-
-
additional information
?
-
-
enzyme of pentose-phosphate pathway
-
-
-
additional information
?
-
-
enzyme of pentose-phosphate pathway
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Ribulose 5-phosphate
D-Xylulose 5-phosphate
show the reaction diagram
-
interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the Calvin cycle and in the oxidative pentose phosphate pathway
-
r
additional information
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
enzyme is involved in carbohydrate metabolism
-
-
-
additional information
?
-
-
enzyme is integral to both the Calvin cycle and the oxidative pentose phosphate pathway
-
-
-
additional information
?
-
-
enzyme of nonoxidative section of the pentose phosphate pathway
-
-
-
additional information
?
-
-
enzyme of pentose-phosphate pathway
-
-
-
additional information
?
-
-
enzyme of pentose-phosphate pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
Co2+ is able to activate the enzyme in vitro
Fe2+
Q96AT9
RPE uses Fe2+ for catalysis
Fe2+
-
the enzyme employs a ferrous iron atom as a solvent-exposed cofactor
Mg2+
Q9A1H8, -
assay carried out at 10 mM Mg2+
Zn2+
-
Zn2+ is able to activate the enzyme in vitro
Mn2+
-
manganese can activate the enzyme in vitro in place of iron converting the enzyme to a form that is unaffected by H2O2
additional information
-
no requirement for a divalent metal ion in catalysis
additional information
-
Ca2+, Cd2+, Cu2+, Mg2+, and Ni2+ do not activate the enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cu(CH3COO)2
-
-
D-deoxyribose 5-phosphate
-
-
DL-alpha-glycerophosphate
-
competitive
-
iodoacetate
-
weak
NEM
-
weak
potassium phosphate
-
weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Zn2+
Q9A1H8, -
RPE is activated by Zn2+ which binds with a stoichiometry of one ion per polypeptide
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
D-ribulose 5-phosphate
-
-
0.2
-
D-ribulose 5-phosphate
Q9A1H8, -
-
0.22
-
D-ribulose 5-phosphate
-
wild-type enzyme
0.22
-
D-ribulose 5-phosphate
-
25C, pH 8.0
0.25
-
D-ribulose 5-phosphate
-
; pH 7.5
0.28
-
D-ribulose 5-phosphate
-
mutant enzyme D186N
0.3
-
D-ribulose 5-phosphate
-
mutant enzyme D186E
1.5
-
D-ribulose 5-phosphate
-
-
2.1
-
D-ribulose 5-phosphate
-
mutant enzyme D186A
15
-
D-ribulose 5-phosphate
-
D-xylulose 5-phosphate
2.4
-
D-ribulose-5-phosphate
-
-
2.9
-
D-ribulose-5-phosphate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00033
-
D-ribulose 5-phosphate
-
mutant enzyme D186A
0.13
-
D-ribulose 5-phosphate
-
mutant enzyme D186N
0.138
-
D-ribulose 5-phosphate
-
-
1.1
-
D-ribulose 5-phosphate
-
mutant enzyme D186E
100
-
D-ribulose 5-phosphate
Q9A1H8, -
RPE metal-free, stoichiometry of Zn2+: 0.1 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate
200
-
D-ribulose 5-phosphate
Q9A1H8, -
mutant H34A, + 10 micromol/l ZnCl2
270
-
D-ribulose 5-phosphate
Q9A1H8, -
mutant H67A, + 10 micromol/l ZnCl2
480
-
D-ribulose 5-phosphate
Q9A1H8, -
RPE as isolated, stoichiometry of Zn2+: 0.3 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate
840
-
D-ribulose 5-phosphate
Q9A1H8, -
RPE as isolated + 0.5 mM ZnCl2 present in assay, stoichiometry of Zn2+: 0.9 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate
870
-
D-ribulose 5-phosphate
Q9A1H8, -
RPE metal-free + 0.5 mM ZnCl2 present in assay, stoichiometry of Zn2+: 0.9 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate
1300
-
D-ribulose 5-phosphate
-
-
7100
-
D-ribulose 5-phosphate
-
wild-type enzyme
1300
-
D-xylulose 5-phosphate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.9
-
DL-alpha-glycerophosphate
-
25C, pH 8.0
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
7.6
-
-
7.5
-
Q9A1H8, -
assay at
8.3
-
-
; reaction with D-ribulose 5-phosphate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9
-
pH 6.5: about 90% of maximal activity, pH 9.0: 95% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pigeon
-
-
Manually annotated by BRENDA team
additional information
-
similar growth rates between the strains and identical soluble proteomes for wild-type and zwf mutant strains grown autotrophically or mixotrophically, twice the amount of xylulose-5-phosphate is synthesized during the Calvin cycle relative to ribose-5-phosphate in mixotrophical growth, with the epimerase being downregulated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
stroma; stroma, 90% of the total epimerase is associated with thylakoid membranes
Manually annotated by BRENDA team
-
nearest neighbor analyses of immunocytolocalization experiments indicate that glyceraldehyde-3-P dehydrogenase and phosphoribulokinase are located close to xylulose-5-P 3-epimerase in the pea leaf chloroplast stroma
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
gel filtration
45000
-
-
gel filtration
45900
-
-
ultracentrifugation
50000
-
-
sedimentation equilibrium experiments
55000
-
-
cyt-RPEase, gel filtration
180000
-
-
gel filtration
200000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 25966, calculation from nucleotide sequence
dimer
-
2 * 22900, SDS-PAGE
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 24300, cyt-RPEase, calculation from nucleotide sequence
hexamer
-
the thgree asymmetric subunits A, B and C for the hexamer by associating with subunits B, A, and C, respectively
octamer
-
8 * 23000, SDS-PAGE
octamer
-
8 * 25000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, using 25% (w/v) PEG 3350, 100 mM Bis-Tris (pH 5.5), and 200 mM NaCl
Q96AT9
crystals are produced with hanging drop method using 6 mg/ml cytosolic enzyme, 1.0 M ammonium sulfate, 50 mM Mops, pH 7.5, 1% w/v polyethylene glycol 400, 10 mM glycerol-3-phosphate and 5 mM L-arginine in the drop
-
hanging drop vapor diffusion method
-
crystal structure of the RPE is solved at 1.8 A resolution in the presence of D-xylitol 5-phosphate, an inert analogue of the D-xylulose 5-phosphate substrate. This structure suggests that the 2,3-enediolate intermediate in the 1,1-proton transfer reaction is stabilized by bidentate coordination to the Zn2+ that also is liganded to His 34, Asp 36, His 67, and Asp 176, the carboxylate groups of the Asp residues are positioned also to function as the acid/base catalysts
Q9A1H8, -
crystals are grown using the microbatch technique from 22% methyl ether PEG 2000, 200 mM MgCl2, 100 mM MES pH 6.0. The crystals belong tp space group P2(1), with unit-cell parameters a = 82.6 A, b = 87.8 A, c = 97.8 A, beta = 114.6, 1.6 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
24 h, 25C, about 70% loss of activity
7
8
-
24 h, 25C, stable
9
-
-
24 h, 25C, about 20% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
2 min, stable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ribulose-5-phosphate 3-epimerase is vulnerable to H2O2 damage in vivo. H2O2 rapidly oxidizes the Fe2+ in a Fenton reaction, the oxidized iron is released immediately, causing a loss of activity. When purified enzyme is loaded with Mn2+, Co2+, or Zn2+, there is no loss in activity when challenged with H2O2
-
716784
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.5 M ammonium sulfate, stable for at least 2 months
-
4C, stable as ammonium precipitate for several weeks
-
2C, wether in crude extracts or highly purified, the recombinant enzyme is inherently unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial
-
Ni-affinity column chromatography and Superdex G75 gel filtration
Q96AT9
recombinant cytosolic enzyme
-
mutant enzymes D186A, D186N, D186E
-
lysate is applied to a chelating sepharose fast flow column charged with Ni2+, the N-terminal His tag is removed by thrombin cleavage
Q9A1H8, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Escherichia coli clones harboring the cfxE gene show up to 19-fold-higher activities of ribulose-phosphate 3-epimerase
-
enzyme with half normal activity in a malformed and severely mentally retarded girl with a de novo interstitial deletion 46,XX.del(2)(q32.lq34). It is suggested that the gene for ribulose-phosphate 3-epimerase is located on the segment 2q32.1 to q34
-
expressed in Escherichia coli BL21(DE3) cells
Q96AT9
expression of cytosoli enzyme in Escherichia coli
-
the enzyme for ribulose 5-phosphate epimerase is localized to chromosome X
-
expression in Escherichia coli
-
expression in Escherichia coli
-
the gene encoding RPE is expressed in the Escherichia coli strain BL21 (DE3)
Q9A1H8, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the growth condition-dependent enzyme is present in the proteomes of wild-type and zwf strains and is downregulated under mixotrophic growth conditions
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D175A
Q96AT9
inactive
D37A
Q96AT9
the mutation almost abolishes the enzymatic activity
H35A
Q96AT9
the mutation almost abolishes the enzymatic activity
H70A
Q96AT9
completely insoluble
L12A
Q96AT9
the mutation results in more than 50% decrease in the activity
M141A
Q96AT9
the mutation results in about 30% decrease in the activity
M39A
Q96AT9
the mutation results in about 10% decrease in the activity
M72A
Q96AT9
the mutation results in an almost 50% decrease in the activity
S10A
Q96AT9
the mutation almost abolishes the enzymatic activity
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
D176A
Q9A1H8, -
no detectable activity, substrate= 10 mM D-ribulose 5-phosphate
D36A
Q9A1H8, -
no detectable activity, substrate= 10 mM D-ribulose 5-phosphate
H34A
Q9A1H8, -
mutant discloses decreased affinity for Zn2+, kcat = 200/sec, substrate = 10 mM D-ribulose 5-phosphate, +10 micromol/l ZnCl2
H67A
Q9A1H8, -
mutant discloses decreased affinity for Zn2+, kcat = 270/sec, substrate = 10 mM D-ribulose 5-phosphate, +10 micromol/l ZnCl2
additional information
Q9A1H8, -
H34A, D36A, H67A, and D176A mutants are constructed since these His and Asp residues are strictly conserved in all RPEs and are observed to coordinate Zn2+ in the reported structures of the RPE from rice
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
spectrophotometric assay for D-ribulose-5-phosphate 3-epimerase and D-ribose-5-phosphate ketol-isomerase
analysis
-
direct assay procedure which exploits differences in CD spectrum between ribulose 5-phosphate and xylulose 5-phosphate
analysis
-
spectrophotometric assay for D-ribulose-5-phosphate 3-epimerase and D-ribose-5-phosphate ketol-isomerase
synthesis
-
enzyme is involved in a cascade of eleven immobilized enzyme reactors in series used for the production of D-ribulose-1,5-bisphosphate from 3-phospho-D-glycerate
analysis
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spectrophotometric assay for D-ribulose-5-phosphate 3-epimerase and D-ribose-5-phosphate ketol-isomerase
analysis
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spectrophotometric determination of ribulose 5-phosphate 3-epimerase in tissue extract