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Information on EC 1.1.99.28 - glucose-fructose oxidoreductase
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EC Tree
1.1.99.28 glucose-fructose oxidoreductaseIUBMB Comments
D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP+.
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Word Map
- 1.1.99.28
- zymomonas
- mobilis
- sorbitol
-
gluconic
-
lactobionic
-
nadp-containing
- gluconolactonase
- d-xylose
- 1,5-anhydro-d-fructose
- synthesis
-
dihydrodiol
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
gfor, glucose-fructose oxidoreductase, gfod2, nadp(h)-dependent glucose-fructose oxidoreductase, glucose fructose oxidoreductase, glucose-fructose oxidoreductase domain containing 2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.1.99
GFOR
glucose fructose oxidoreductase
glucose-fructose oxidoreductase
Glucose-fructose transhydrogenase
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-
-
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Transhydrogenase, glucose-fructose
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-
-
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GFOR
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + D-fructose = D-gluconolactone + D-glucitol
ping-pong mechanism with a single site for all substrates, two half-reactions with alternate reduction of NADP+ and oxidation of NADPH
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D-glucose + D-fructose = D-gluconolactone + D-glucitol
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-Glucose:D-fructose oxidoreductase
D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP+.
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CAS REGISTRY NUMBER
COMMENTARY
94949-35-6
-
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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-Galactose + D-fructose
?
-
at 8% of the activity relative to D-glucose
-
-
?
D-Glucose + dihydroxyacetone
?
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at 6% of the activity relative to fructose
-
-
?
D-Glucose + L-sorbose
?
-
at 0.5% of the activity relative to fructose
-
-
?
D-Mannose + D-fructose
?
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at 12% of the activity relative to D-glucose
-
-
?
DL-Glyceraldehyde + D-fructose
?
-
at 1.5% of the activity relative to D-glucose
-
-
?
L-Arabinose + D-fructose
?
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at 3% of the activity relative to D-glucose
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-
?
2-Deoxy-D-glucose + D-fructose
?
-
at 16% of the activity relative to D-glucose
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-
?
2-Deoxy-D-glucose + D-fructose
?
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at 6% of the activity relative to D-glucose
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-
?
D-Glucose + D-fructose
?
-
enzyme is responsible for sorbitol production
-
-
?
D-Glucose + D-fructose
?
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the enzyme produces the solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone and thereby protects the bacterium against osmotic shock in sugar-rich environment
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-glucitol
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-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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-
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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a variable pH from 7.8 to 6.4 and a constant temperature of about 47°C are the best conditions for achieving good conversion yields and productivities
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
at pH 6.4 and 39°C when 700 mM lactose/350 mM fructose pair substrate is used, the maximum possible conversion yield is attained after 24 h of operation
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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from pineapple juice, at optimal conditions a maximum of 80% (w/v) sugar conversion is obtained
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-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
a variable pH from 7.8 to 6.4 and a constant temperature of about 47°C are the best conditions for achieving good conversion yields and productivities
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
at pH 6.4 and 39°C when 700 mM lactose/350 mM fructose pair substrate is used, the maximum possible conversion yield is attained after 24 h of operation
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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-
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
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-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
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-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
-
-
-
-
?
D-glucose + D-fructose + H2O
D-glucono-1,5-lactone + D-sorbitol
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pineapple juice sugars, the enzyme is efficient in converting juice sugars of fruits juices having higher natural pH
-
-
?
D-glucose + D-fructose + H2O
D-glucono-1,5-lactone + D-sorbitol
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pineapple juice sugars, the enzyme is efficient in converting juice sugars of fruits juices having higher natural pH
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?
additional information
?
-
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in periplasm the enzyme functions to produce sorbitol for osmoprotection
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-
?
additional information
?
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decreasing enzyme/substrate affnities are observed when D-fructose is in the mixture with D-glucose, D-maltose, D-galactose, and lactose
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-
?
additional information
?
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decreasing enzyme/substrate affnities are observed when D-fructose is in the mixture with D-glucose, D-maltose, D-galactose, and lactose
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-
?
additional information
?
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glucose-fructose oxidoreductase oxidizes not only glucose but also seven other aldose sugars to produce the corresponding organic acids; in particular, lactose is oxidized to lactobionic acid
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?
additional information
?
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glucose-fructose oxidoreductase oxidizes not only glucose but also seven other aldose sugars to produce the corresponding organic acids; in particular, lactose is oxidized to lactobionic acid
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-
?
additional information
?
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glucose-fructose oxidoreductase oxidizes not only glucose but also seven other aldose sugars to produce the corresponding organic acids; in particular, lactose is oxidized to lactobionic acid
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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
D-Glucose + D-fructose
?
-
enzyme is responsible for sorbitol production
-
-
?
D-Glucose + D-fructose
?
-
the enzyme produces the solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone and thereby protects the bacterium against osmotic shock in sugar-rich environment
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
-
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
a variable pH from 7.8 to 6.4 and a constant temperature of about 47°C are the best conditions for achieving good conversion yields and productivities
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
at pH 6.4 and 39°C when 700 mM lactose/350 mM fructose pair substrate is used, the maximum possible conversion yield is attained after 24 h of operation
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
from pineapple juice, at optimal conditions a maximum of 80% (w/v) sugar conversion is obtained
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
a variable pH from 7.8 to 6.4 and a constant temperature of about 47°C are the best conditions for achieving good conversion yields and productivities
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
at pH 6.4 and 39°C when 700 mM lactose/350 mM fructose pair substrate is used, the maximum possible conversion yield is attained after 24 h of operation
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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-
-
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?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
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-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
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-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
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-
-
-
?
D-glucose + D-fructose
D-gluconolactone + D-glucitol
-
-
-
-
?
D-glucose + D-fructose + H2O
D-glucono-1,5-lactone + D-sorbitol
-
pineapple juice sugars, the enzyme is efficient in converting juice sugars of fruits juices having higher natural pH
-
-
?
D-glucose + D-fructose + H2O
D-glucono-1,5-lactone + D-sorbitol
-
pineapple juice sugars, the enzyme is efficient in converting juice sugars of fruits juices having higher natural pH
-
-
?
additional information
?
-
-
in periplasm the enzyme functions to produce sorbitol for osmoprotection
-
-
?
additional information
?
-
-
decreasing enzyme/substrate affnities are observed when D-fructose is in the mixture with D-glucose, D-maltose, D-galactose, and lactose
-
-
?
additional information
?
-
-
decreasing enzyme/substrate affnities are observed when D-fructose is in the mixture with D-glucose, D-maltose, D-galactose, and lactose
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NAD+
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NAD+
S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity
NADP+
-
tightly bound as hydrogen carrier
NADP+
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NADP+
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NADPH/NADP+
NADP+
S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity
NADPH
-
tightly bound as hydrogen carrier
NADPH
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NADPH
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NAD(P)H/NAD(P)+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aldonolactone
-
the interaction of the enzyme with the aldonolactone product triggers a sequential process that affects the protein structure conformationally and chemically and results in an irreversible loss of activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypercholesterolemia
Effect of a GFOD2 variant on responses in total and LDL cholesterol in Mexican subjects with hypercholesterolemia after soy protein and soluble fiber supplementation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes
-
additional information
additional information
-
kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes
additional information
-
kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
6.4
7.8 - 8.2
-
higher enzymatic activities in immobilized permeabilized cells are obtained at pH 7.8 and 8.2 which are 80% higher than at pH 6.4
6.2
-
without pH control, the enzyme is inactivated rapidly due to gluconic acid formation
6.4
-
the enzymatic complex glucose-fructose oxidoreductase/glucono-delta-lactonase is most active at pH 6.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.1
-
pH 5.0: about 35% of maximal activity, pH 7.1: about 30% of maximal activity
5.6 - 7.4
-
at pH 5.6 and 7.4 there are still 65% of enzyme activity remaining
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47 - 50
-
higher enzymatic activities in immobilized permeabilized cells are obtained at 47 and 50°C which are 80% higher than at 39°C, respectively
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44 - 52
-
an increase of approximately 35% in the enzymatic activity in immobilized permeabilized cells is observed between 44 and 52°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
translocated across the membrane in fully folded form. A twin-arginine motif in the signal peptide directs it to a Sec-independent pathway by which it is translocated, in fully folded form, into the periplasm where it functions to produce sorbitol for osmoprotection
brenda
-
-
-
brenda
-
the efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
lactobionic acid is catalyzed by the enzymes glucose-fructose oxidoreductase and glucono-delta-lactonase of Zymomonas mobilis
metabolism
-
lactobionic acid is catalyzed by the enzymes glucose-fructose oxidoreductase and glucono-delta-lactonase of Zymomonas mobilis
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM