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Information on EC 5.3.1.27 - 6-phospho-3-hexuloisomerase
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5.3.1.27 6-phospho-3-hexuloisomeraseIUBMB Comments
This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, 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 . The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme .
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Word Map
- 5.3.1.27
- formaldehyde
- monophosphate
- ribulose
-
rump
- methanol
-
nonmethylotrophic
- methanolicus
- gastri
-
feedstock
-
formaldehyde-fixing
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one-carbon
- synthesis
- pentose
- fructose-6-phosphate
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methylotrophy
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dissimilation
- pyrococcus
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hyperthermophilic
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nad-dependent
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corynebacterium
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methylomonas
- glutamicum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
6-phospho-3-hexuloisomerase, 3-hexulose-6-phosphate isomerase, phospho-3-hexuloisomerase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hexulose-6-phosphate isomerase
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6-phospho-3-hexuloisomerase
Hpi1
Hpsi2
HxlB
PHI
phospho-3-hexuloisomerase
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-
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YckF
[acyl-carrier protein]:acetate ligase
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6-phospho-3-hexuloisomerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabino-hex-3-ulose 6-phosphate = D-fructose 6-phosphate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-arabino-hex-3-ulose-6-phosphate isomerase
This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, 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 EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
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?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
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?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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?
additional information
?
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enzyme is specific for substrates D-arabino-3-hexulose 6-phosphate and D-fructose 6-phosphate
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?
additional information
?
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no substrate: D-ribulose 5-phosphate, D-xylulose 5-phosphate or D-allulose 6-phosphate
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?
additional information
?
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bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase is essential for the biosynthesis of ribulose 5-phosphate. The ribulose monophosphate pathway substitutes for the classical pentose phosphate pathway in Thermococcus kodakarensis
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase is essential for the biosynthesis of ribulose 5-phosphate. The ribulose monophosphate pathway substitutes for the classical pentose phosphate pathway in Thermococcus kodakarensis
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?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
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-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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at 1 mm sugar phosphate concentration, D-allulose 6-phosphate, D-fructose 6-phosphate, 6-phospho-D-gluconate, D-ribulose 5-phosphate, D-xylulose 5-phosphate, D-erythrose 4-phosphate and glyceraldehyde 3-phosphate do not affect the isomerase activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
formaldehyde
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concomitant induction of 3-hexulose 6-phosphate synthase and 6-phospho-3-hexuloisomerase by formaldehyde
additional information
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no induction by by methanol, formate, or methylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
154
3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerasefusion enzyme, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
both recombinant 6-phospho-3-hexuloisomerase and 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase fusion enzyme
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
concomitant induction of 3-hexulose 6-phosphate synthase and 6-phospho-3-hexuloisomerase by formaldehyde
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brenda
hexulose-6-phosphate synthase, activity of EC 4.1.2.43, and isomerase
UniProt
brenda
hexulose-6-phosphate synthase, activity of EC 4.1.2.43, and isomerase
UniProt
brenda
bifunctional 3-hexulose 6-phosphate synthase/6-phospho-3-hexuloisomerase, constitutive expression
UniProt
brenda
bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi (Hpsi2). Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively. the fusion protein Hpsi2 does not show isomerase activity, but the sequences corresponding to its HPS and PHI regions, when expressed separately, produce active enzymes
physiological function
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi. Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively
physiological function
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6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
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physiological function
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6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
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physiological function
-
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi. Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively
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physiological function
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3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi (Hpsi2). Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively. the fusion protein Hpsi2 does not show isomerase activity, but the sequences corresponding to its HPS and PHI regions, when expressed separately, produce active enzymes
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physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
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physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
-
Show AA Sequence and Transmembrane Helices (542 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
21475
4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain
42000
x * 42000, recombinant 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerasefusion enzyme
47000
4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain
21000
4 * 21000, SDS-PAGE, recombinant 6-phospho-3-hexuloisomerase
21000
4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
?
x * 42000, recombinant 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerasefusion enzyme
?
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x * 42000, recombinant 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerasefusion enzyme
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dimer
2 * 20000, SDS-PAGE, 2 * 19200, calculated from sequence
dimer
2 * 40000, SDS-PAGE, 2 * 41900, calculated from sequence
dimer
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2 * 20000, SDS-PAGE, 2 * 19200, calculated from sequence
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dimer
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2 * 40000, SDS-PAGE, 2 * 41900, calculated from sequence
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tetramer
4 * 21000, SDS-PAGE, recombinant 6-phospho-3-hexuloisomerase
tetramer
4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 2.0 A resolution. MJ1247 is an alpha/beta structure consisting of a five-stranded parallel beta-sheet flanked on both sides by alpha-helices, forming a three-layered alpha-beta-alpha sandwich. The fold represents the nucleotide binding motif of a flavodoxin type. Protein forms a tetramer in the crystal an in solution and each monomer has a folding similar to the isomerase domain of glucosamine 6-phosphate synthase
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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gene disruption causes moderate sensitivity to formaldehyde
additional information
fusion gene construct of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. The gene product of 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase exhibits both activities at room temperature and catalyzes the sequential reactions more efficiently than a simple mixture of the individual enzymes. The gene product of 6-phospho-3-hexuloisomerase /3-hexulose-6-phosphate synthase fails to display any enzyme activity. Escherichia coli strains harboring the 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase gene consume formaldehyde more efficiently and exhibited better growth in a formaldehyde containing medium than the host strain
additional information
-
fusion gene construct of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. The gene product of 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase exhibits both activities at room temperature and catalyzes the sequential reactions more efficiently than a simple mixture of the individual enzymes. The gene product of 6-phospho-3-hexuloisomerase /3-hexulose-6-phosphate synthase fails to display any enzyme activity. Escherichia coli strains harboring the 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase gene consume formaldehyde more efficiently and exhibited better growth in a formaldehyde containing medium than the host strain
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additional information
expression of the full-length gene encoding the hybrid enzyme 3-hexulose 6-phosphate synthase/6-phospho-3-hexuloisomerase, the sequence corresponding to the 3-hexulose 6-phosphate synthase region, and the sequence corresponding to the 6-phospho-3-hexuloisomerase region produces active enzymes in Escherichia coli. The bifunctional enzyme catalyzes the sequential reaction much more efficiently than a mixture of the isolated domains
additional information
-
expression of the full-length gene encoding the hybrid enzyme 3-hexulose 6-phosphate synthase/6-phospho-3-hexuloisomerase, the sequence corresponding to the 3-hexulose 6-phosphate synthase region, and the sequence corresponding to the 6-phospho-3-hexuloisomerase region produces active enzymes in Escherichia coli. The bifunctional enzyme catalyzes the sequential reaction much more efficiently than a mixture of the isolated domains
additional information
-
deletion of bifunctional 3-hexulose-6-phosphate synthase /6-phospho-3-hexuloisomerase results in loss of growth in minimal medium, which can be recovered by addition of nucleosides to the medium
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
half-life above 90 min, bifunctional enzyme. Half-life below 5 min, separately expressed 6-phospho-3-hexuloisomerase domain
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, l0 mM-Tris-HCI, 1 mM-EDTA buffer, pH 7.5, stable for 4 months
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0-4°C, l0 mM-Tris-HCI, 1 mM-EDTA buffer, pH 7.5, stable for 4 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 3-hexulose-6-phosphate synthase/6-phosphate-3-hexuloisomerase fusion protein is expressed in chloroplasts of geranium (Pelargonium sp. Frensham)
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expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis