Information on EC 4.1.2.43 - 3-hexulose-6-phosphate synthase

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

EC NUMBER
COMMENTARY hide
4.1.2.43
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RECOMMENDED NAME
GeneOntology No.
3-hexulose-6-phosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde assimilation II (RuMP Cycle)
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formaldehyde oxidation I
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Metabolic pathways
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Methane metabolism
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Microbial metabolism in diverse environments
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pentose phosphate pathway
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Pentose phosphate pathway
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ribulose monophosphate pathway
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SYSTEMATIC NAME
IUBMB Comments
D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming)
Requires Mg2+ or Mn2+ for maximal activity [1]. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal [7]. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds [1]. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase [6]. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily [5].
CAS REGISTRY NUMBER
COMMENTARY hide
55576-36-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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strain C2A1
UniProt
Manually annotated by BRENDA team
C2A1
strain C2A1
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain MB58
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-
Manually annotated by BRENDA team
strain MB58
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-
Manually annotated by BRENDA team
strain MGA3
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-
Manually annotated by BRENDA team
strain MGA3
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-
Manually annotated by BRENDA team
strain C1
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Manually annotated by BRENDA team
strain S1
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Manually annotated by BRENDA team
strain S1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Fusaro
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain KT, obligate methylotroph
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Manually annotated by BRENDA team
strain GBS
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Manually annotated by BRENDA team
strain GI33
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Manually annotated by BRENDA team
strain W6
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Manually annotated by BRENDA team
strain W6
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain OT3
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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bifunctional enzyme
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 + acetaldehyde
?
show the reaction diagram
D-ribulose 5-phosphate + benzaldehyde
?
show the reaction diagram
D-ribulose 5-phosphate + bromoacetaldehyde
?
show the reaction diagram
D-ribulose 5-phosphate + butyraldehyde
?
show the reaction diagram
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-
-
?
D-ribulose 5-phosphate + chloral
?
show the reaction diagram
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?
D-ribulose 5-phosphate + chloroacetaldehyde
?
show the reaction diagram
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-
-
-
?
D-ribulose 5-phosphate + chloropropionaldehyde
?
show the reaction diagram
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-
-
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?
D-ribulose 5-phosphate + dichloroacetaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + DL-glyceraldehyde
?
show the reaction diagram
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-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
D-ribulose 5-phosphate + glutaraldehyde
?
show the reaction diagram
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-
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?
D-ribulose 5-phosphate + glycolaldehyde
4-heptulose 7-phosphate
show the reaction diagram
D-ribulose 5-phosphate + glycolaldehyde
?
show the reaction diagram
D-ribulose 5-phosphate + glyoxal
?
show the reaction diagram
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-
-
-
?
D-ribulose 5-phosphate + isobutyraldehyde
?
show the reaction diagram
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-
-
-
?
D-ribulose 5-phosphate + isovaleraldehyde
?
show the reaction diagram
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-
?
D-ribulose 5-phosphate + methylglyoxal
?
show the reaction diagram
D-ribulose 5-phosphate + methylmercaptopropionaldehyde
?
show the reaction diagram
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?
D-ribulose 5-phosphate + propionaldehyde
?
show the reaction diagram
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?
D-ribulose 5-phosphate + pyridine-2-carboxaldehyde
?
show the reaction diagram
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?
D-ribulose 5-phosphate + pyridine-3-carboxaldehyde
?
show the reaction diagram
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?
D-ribulose 5-phosphate + pyridine-4-carboxaldehyde
?
show the reaction diagram
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?
D-ribulose 5-phosphate + valeraldehyde
?
show the reaction diagram
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?
additional information
?
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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-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
the enzyme activity is also promoted with 1 mM Cd2+
Cu2+
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33% stimulation of activity at 1 mM
Ni2+
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97% stimulation of activity at 1 mM
sulfate
the active site of each HPS monomer contains a sulfate ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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49% inhibition at 1 mM
D-ribulose 5-phosphate
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commercial D-ribulose 5-phosphate inhibits the enzyme
Glutaraldehyde
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22% inhibition at 4 mM
glyceraldehyde
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13% inhibition at 4 mM
glycolaldehyde
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49% inhibition at 4 mM
glycolic acid
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glycolic acid inhibits the enzyme competitively with respect to formaldehyde
glyoxylate
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12% inhibition at 4 mM
Hg2+
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81% inhibition with 1 mM Hg2+
methylglyoxal
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26% inhibition at 4 mM
Ni2+
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64% inhibition at 1 mM
o-phenanthroline
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the enzyme is completely inhibited by the presence of 2 mM o-phenanthroline
Pb2+
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48% inhibition with 1 mM Pb2+
Tiron
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the enzyme is completely inhibited by the presence of 2 mM tiron
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
formaldehyde
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expression of the HPS coding hxlAB operon is induced by the presence of formaldehyde
HxlR
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necessary for formaldehyde-induced expression of the HPS coding hxlAB operon
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
D-arabino-hex-3-ulose 6-phosphate
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in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 30C
0.0045 - 1.6
D-ribulose 5-phosphate
0.00147 - 2.96
formaldehyde
4.3
glycolaldehyde
5.7
methylglyoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
62.2 - 159
formaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.4
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cell free extract, at 30C
1.71
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cell free extract, at 30C
3.2
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cell free extract, at 30C
3.3
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cell free extract
3.5
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cell free extract, at 50C
4.4
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hexulose-6-phosphate synthase activity of the gene product Fae-Hps, at 30C, pH 7.0
4.5
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crude extract, at 30C
9.8
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cell free extract
20
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purified enzyme
26
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crude extract
41.1
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cell free extract, recombinant HPS
52
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after 16fold purification
56.7
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crude cell extract
66.5
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after 14.8fold purification, at 30C
69
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after 41fold purification, at 30C
70.9
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after 1.73fold purification, recombinant HPS
74.2
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after 23fold purification, at 30C
148
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after 15.1fold purification
235
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after 4.14fold purification
4100
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after 161fold purification
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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purified recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
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SDS-PAGE
24000
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SDS-PAGE
25000
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recombinant HPS, gel filtration
42000
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SDS-PAGE
47000
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sedimentation velocity
80000
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gel filtration
162000
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EDTA-solubilized HPS-PHI fusion enzyme, gel filtration
310000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homohexamer
homotetramer
monomer
additional information
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multiple forms of the enzyme may be responsible for the generation of the complex shape, and thus, the kinetic characteristic should he the sum of differing characteristics
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with a sulfate ion, sitting drop vapor diffusion method, using 18% (w/v) polyethylene glycol (PEG) 3350 and 0.2 M MgCl2
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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remains stable at pH 6.0-8.0 at 30C for 1 h, enzyme stability decreases at pH values below 6.0
694012
7 - 8
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stable in neutral to slightly alkaline solutions
691118
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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remains stable in the pH range of 6.5-7.5 at 30C for 6 h
40 - 60
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no decrease in activity is observed within 6 h at 40C in the presence of 5 mM MgCl2, at 50C and 60C the enzyme is stable for 2.5 and 0.5 h, respectively, one-half the initial activities are found after 6 and 1.5 h respectively
40 - 80
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almost full activity is retained after incubation at 40C for 30 min, whereas at 80C for 10 min the enzyme is completely inactivated
55 - 65
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the enzyme retains more than 50% of its activity at 55C after 1 h, the enzyme retains more than 50% of its activity at 65C after 30 min
60
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3-hexulose phosphate synthase is rapidly inactivated at elevated temperatures, activity is totally lost within 5 min at 60C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, in the presence of 2.5 mM MgCl2, 6 months, remains stable unless repeatedly frozen and thawed
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-20C, purified enzyme, at least 1 year, no loss of activity
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-80C, purified enzyme, in the presence of 5 mM MgSO4, 5 mM D-ribose 5-phosphate, and 1.75 units/ml phosphoriboisomerase, at least 5 months, no loss of activity
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0C to -4C, purified enzyme in the presence of 3.2 M ammonium sulfate, at least 1 year, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G-100 gel filtration
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ammonium sulfate precipitation, DEAE-cellulose column chromatography
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DEAE-cellulose column chromatography, DEAE-Sephadex A-50 gel filtration, and Sephadex G-75 gel filtration
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DEAE-cellulose column chromatography, hydroxylapatite column chromatography, Sephadex G-150 gel filtration, Sephadex G-100 gel filtration, and DEAE-Sephadex A-50 gel filtration
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DEAE-Sephacel column chromatography, Q-Sepharose column chromatography, and hydroxyapatite column chromatography
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DEAE-Toyopearl column chromatography butyl-Toyopearl column chromatography
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DEAE-Toyopearl column chromatography, butyl-Toyopearl column chromatography, and ammonium sulfate precipitation
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Ni-chelating Sepharose column chromatography
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phenyl-Sepharose column chromatography and DEAE-Sephacel column chromatography
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phenyl-Sepharose column chromatography, and DEAE-Sephacel column chromatography
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polyethylene imine precipitation, S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephadex G-75 gel filtration
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Q-Sepharose column chromatography, phenyl-Superose column chromatography, Superose 12 chromatography, and Sephadex G-25 gel filtration
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ultracentrifugation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hexulose-6-phosphate synthase/6-phosphate-3-hexuloisomerase fusion enzyme from Mycobacterium gastri is expressed in chloroplasts of Pelargonium sp.
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expressed in Escherichia coli
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expressed in Escherichia coli BL21 (DE3) cells
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expressed in Escherichia coli BL21 (DE3) pLysS cells
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expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells, HPS only, or as fusion enzyme with 6-phospho-3-hexuloisomerase
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expressed in Escherichia coli Rosetta(DE3) cells
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H134A
the mutation abolishes HPS activity
H134D
the mutation abolishes HPS activity
H134K
the mutation abolishes HPS activity
H134N
the mutation abolishes HPS activity
H134S
the mutation abolishes HPS activity
K61A
the mutant exhibits 50-90% of the activity of the wild type enzyme
K61D
the mutant exhibits 50-90% of the activity of the wild type enzyme
K61H
the mutant exhibits 50-90% of the activity of the wild type enzyme
K61S
the mutant exhibits 50-90% of the activity of the wild type enzyme
H134A
-
the mutation abolishes HPS activity
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H134D
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the mutation abolishes HPS activity
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H134K
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the mutation abolishes HPS activity
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H134N
-
the mutation abolishes HPS activity
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K61A
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the mutant exhibits 50-90% of the activity of the wild type enzyme
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
synthesis
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