Information on EC 5.3.1.27 - 6-phospho-3-hexuloisomerase

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

EC NUMBER
COMMENTARY hide
5.3.1.27
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RECOMMENDED NAME
GeneOntology No.
6-phospho-3-hexuloisomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabino-hex-3-ulose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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 (oxidative branch) II
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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 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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain 77a
UniProt
Manually annotated by BRENDA team
no activity in Hansenula polymorpha
strain DL-1
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Manually annotated by BRENDA team
no activity in Hansenula polymorpha DL-1
strain DL-1
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Manually annotated by BRENDA team
no activity in Kloeckera sp.
strain 2201
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Manually annotated by BRENDA team
no activity in Kloeckera sp. 2201
strain 2201
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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
strain 77a
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Manually annotated by BRENDA team
strain 77a
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
D-arabino-3-hexulose 6-phosphate
D-fructose-6-phosphate
show the reaction diagram
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
D-fructose 6-phosphate
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
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r
D-fructose 6-phosphate
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
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-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
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1 mM, 35% residual activity
Cu2+
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1 mM, 8% residual activity
Mg2+
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5 mM, 30% loss of activity
Ni2+
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1 mM, 14% residual activity
Zn2+
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1 mM, 40% residual activity
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 hide
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 hide
LITERATURE
IMAGE
0.1
D-arabino-3-hexulose 6-phosphate
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30C, pH 7.0
0.029
D-arabino-hex-3-ulose 6-phosphate
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pH 7.0, 30C
0.67 - 1.1
D-fructose 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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pH 7.0, 30C
154
3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerasefusion enzyme, 30C
563
6-phospho-3-hexuloisomerase, 30C
1560
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30C, pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
separately expressed 6-phospho-3-hexuloisomerase domain
80 - 85
bifunctional enzyme
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
67000
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gel filtration
75000
separately expressed 6-phospho-3-hexuloisomerase domain
94000
gel filtration, recombinant 6-phospho-3-hexuloisomerase
162000
gel filtration, bifunctional enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.7 A, space group P6522 or P6122
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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10 min, complete loss of activity
90
half-life above 90 min, bifunctional enzyme. Half-life below 5 min, separately expressed 6-phospho-3-hexuloisomerase domain
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, l0 mM-Tris-HCI, 1 mM-EDTA buffer, pH 7.5, stable for 4 months
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0-4C, l0 mM-Tris-HCI, 1 mM-EDTA buffer, pH 7.5, stable for 4 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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