Any feedback?
Information on EC 1.1.99.28 - glucose-fructose oxidoreductase and Organism(s) Zymomonas mobilis and UniProt Accession Q07982
for references in articles please use BRENDA:EC1.1.99.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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+.
Specify your search results
Word Map
- 1.1.99.28
- zymomonas
- mobilis
- sorbitol
-
gluconic
-
lactobionic
-
nadp-containing
- gluconolactonase
- d-xylose
- 1,5-anhydro-d-fructose
- synthesis
-
dihydrodiol
The taxonomic range for the selected organisms is: Zymomonas mobilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GFOR
Glucose-fructose transhydrogenase
-
-
-
-
Transhydrogenase, glucose-fructose
-
-
-
-
GFOR
-
-
-
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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+.
CAS REGISTRY NUMBER
COMMENTARY
94949-35-6
-
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 + 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 + dihydroxyacetone
?
-
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
?
-
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
?
-
at 3% of the activity relative to D-glucose
-
-
?
D-glucose + D-fructose
D-glucono-1,5-lactone + D-sorbitol
-
-
?
2-Deoxy-D-glucose + D-fructose
?
-
at 16% of the activity relative to D-glucose
-
-
?
2-Deoxy-D-glucose + D-fructose
?
-
at 6% of the activity relative to D-glucose
-
-
?
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
-
-
?
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
-
-
?
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 + 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
?
-
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
-
-
?
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
-
-
?
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
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
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+
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+
S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity
NADP+
-
tightly bound as hydrogen carrier
NADP+
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NADPH/NADP+
NADPH
-
tightly bound as hydrogen carrier
NADPH
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NAD(P)H/NAD(P)+
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
-
-
-
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
lactobionic acid is catalyzed by the enzymes glucose-fructose oxidoreductase and glucono-delta-lactonase of Zymomonas mobilis
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
40000
-
x * 40000, SDS-PAGE. In recombinant strains a precursur form of the enzyme with MW 45000 accumulates
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
the N-terminal arm is essential for tetramer formation by wild-type GFOR
tetramer
?
-
x * 40000, SDS-PAGE. In recombinant strains a precursur form of the enzyme with MW 45000 accumulates
tetramer
-
each subunit of the tetramer comprises two domains, a classical dinucleotide-binding domain, and a C-terminal domain based on a predominantly antiparallel nine-stranded beta sheet
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
GFOR is synthesized in the cytoplasm with a 52-residue signal peptide, giving a precursor form, preGFOR, that is fully active and has its cofactor tightly bound
proteolytic modification
-
K123A mutant enzyme shows processing behavior comparable to wild-type enzyme, S116D mutant enzyme and S116D/K121A/K123Q/I124K mutant enzyme shows significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min, K121A mutant enzyme is not processed within 60 min
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion in hanging drops, crystal structure of the NAD+ complex of a truncated form of the enzyme, GFORDELTA1-22/S64D, in which the first 22 residues of the N-terminal arm of the mature protein have been deleted, structure refined at 2.7 A resolution shows that the truncated form of the enzyme forms a dimer and implies that the N-terminal arm is essential for tetramer formation by wild-type GFOR
hanging drop method, crystal structure of oxidized preGFOR R30K/R31K, in complex with succinate (preGFOR(succ)) and with glycerol (PreGFOR(gll)), at 2.2 A and 2.05 A resolution, respectively, and of reduced preGFOR R30K/R31K, after incubation with glucose (preGFOR(Glu)) and with sorbitol (preGFOR(sorb)) at 2.5 A and 2.6 A resolution. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-22/S64D
S64D mutation converts the strict NADP+ spoecificity of wild-type GFOR to a dual NADP+/NAD+ specificity
S116D
Y269F
essential acid-base catalyst, involved in substrate binding, activity completely abolished
DELTA32-46
-
the mutant enzyme DELTA32-46 is a protein that is no longer processed but shows full enzymatic activity and has the cofactor firmly bound. The mutant enzyme DELTA2-20 or a mutant enzyme with an exchange of the entire signal sequence with the signal sequence of gluconolactonase of Zymomonas mobilis leads to an active and processed protein
K123A
-
mutant enzyme shows processing behavior comparable to wild-type enzyme
S116D
-
significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min
S116D/K121A/K123Q/I124K
-
significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min
additional information
-
mutant enzymes with deletions in the signal peptide are enzymatically active and contain tightly bound NADP(H). Mutant enzymes with a complete deletion of the signal peptide are produced as cytosolic enzymes
S116D
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
S116D
dual NADP+/NAD+ specificity with loss of tight cofactor binding, wild type: strict NADP+ specificity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39 - 45
-
when measured on its natural substrates (D-fructose and D-glucose), high enzyme thermal stability at 39 and 43°C is observed, with remaining activities close to 100% of the initial, whereas at 45°C, 91% of the activity is maintained
50
-
the enzymatic activity in non-immobilized permeabilized cells is almost completely depleted at 50°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glucose-fructose oxidoreductase (GFOR)/glucono-delta-lactonase (GL) enzyme complex immobilized on Ca-alginate is stable for at least 23 cycles
enzyme activity loss in pineapple juice is even stronger (18%) than in 0.5 M sugar solution
-
guanidinium hydrochloride inactivates by induction of structural transitions that are comparable to that observed during substrate turnover. This leads to time-dependent formation of high-order associates and consequently inactivation
-
in absence of substrates or in presence of only one substrate, either fructose or glucose, the enzyme is fully stable
-
inactivation during substrate turnover. The process of inactivation is triggered by structural transitions that are induced by the lactone product and involves aggregation as the ultimate cause of irreversible inactivation
-
the interaction of the enzyme with the aldonolactone product triggers a sequential process that affects the protein structure conformationally and chemically and, ultimately, results in an irreversible loss of activity
-
thiol reagents stabilize. Dithiothreitol is the most efficient, 5-15 mM
-
urea, 1.0 M, prevents the formation of high-order associates and increases the half-life under operational conditions 10fold
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
NADP+ is required for the enzyme to fold into its native conformation and its absence from the Escherichia coli periplasm is responsible for failure to form a stable periplasmic protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
lactobionic acid production by a glucose-fructose oxidoreductase (GFOR)/glucono-delta-lactonase (GL) enzyme complex
synthesis
-
glucose-fructose oxidoreductase and glucono-delta-lactonase are involved in bioconversion by cell of Zymomonas mobilis, production of sorbitol and gluconic acid. High initial glucose concentration leads to decreasing activities of in fresh cells due to changes in cell wall
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zachariou, M.; Scopes, R.K.
Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production
J. Bacteriol.
167
863-869
1986
Zymomonas mobilis
Kanagasundaram, V.; Scopes, R.K.
Cloning, sequence analysis and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis
J. Bacteriol.
174
1439-1447
1992
Zymomonas mobilis
Hardman, M.J.; Scopes, R.K.
The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis
Eur. J. Biochem.
173
203-209
1988
Zymomonas mobilis
Furlinger, M.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis
Eur. J. Biochem.
251
955-963
1998
Zymomonas mobilis
Hardman, M.J.; Tsao, M.; Scopes, R.K.
Changes in the fluorescence of bound nucleotide during the reaction catalysed by glucose-fructose oxidoreductase from Zymomonas mobilis
Eur. J. Biochem.
205
715-720
1992
Zymomonas mobilis
Wiegert, T.; Sahm, H.; Sprenger, G.A.
The substitution of a single amino acid residue (Ser-116->Asp) alters NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis into a glucose dehydrogenase with dual coenzyme specificity
J. Biol. Chem.
272
13126-13133
1997
Zymomonas mobilis (Q07982), Zymomonas mobilis
Loos, H.; Sahm, H.L.; Sprenger, G.A.
Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas mobilis, is active in its precursor form
FEMS Microbiol. Lett.
107
293-298
1993
Zymomonas mobilis
Wiegert, T.; Sahm, H.; Sprenger, G.A.
Export of the periplasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis
Arch. Microbiol.
166
32-41
1996
Zymomonas mobilis
Furlinger, M.; Nidetzky, B.; Scopes, R.K.; Haltrich, D.; Kulbe, K.D.
Inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis during its catalytic action
Ann. N. Y. Acad. Sci.
799
752-756
1996
Zymomonas mobilis
-
Furlinger, M.; Satory, M.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
Control of the association state of tetrameric glucose-fructose oxidoreductase from Zymomonas mobilis as the rationale for stabilization of the enzyme in biochemical reactors
J. Biochem.
124
280-286
1998
Zymomonas mobilis
Sprenger, G.A.
Die periplasmatische Glukose-Fruktose-Oxidoreduktase aus Zymomonas mobilis
BIOspektrum
3
52-53
1997
Zymomonas mobilis
-
Nidetzky, B.; Furlinger, M.; Gollhofer, D.; Haug, I.; Haltrich, D.; Kulbe, K.D.
Simultaneous enzymatic synthesis of gluconic acid and sorbitol. Production, purification, and application of glucose-fructose oxidoreductase and gluconolactonase
Appl. Biochem. Biotechnol.
63-65
173-188
1997
Zymomonas mobilis
Gollhofer, D.; Nidetzky, B.; Fuerlinger, M.; Kulbe, K.D.
Efficient protection of glucose-fructose oxidoreductase from Zymomonas mobilis against irreversible inactivation during its catalytic action
Enzyme Microb. Technol.
17
235-240
1995
Zymomonas mobilis
-
Wiegert, T.; Sahm, H.; Sprenger, G.A.
Expression of the Zymomonas mobilis gfo gene or NADP-containing glucose:fructose oxidoreductase (GFOR) in Escherichia coli. Formation of enzymatically active preGFOR but lack of processing into a stable periplasmic protein
Eur. J. Biochem.
224
107-112
1997
Zymomonas mobilis
Kingston, R.L.; Scopes, R.K.; Baker, E.N.
The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP
Structure
4
1413-1428
1996
Zymomonas mobilis
Ermler, L.H.; Sprenger, G.A.; Sahm, H.
Crystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis
Protein Sci.
3
2447-2449
1994
Zymomonas mobilis
Nurizzo, D.; Halbig, D.; Sprenger, G.A.; Baker, E.N.
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands
Biochemistry
40
13857-13867
2001
Zymomonas mobilis
Erzinger, G.S.; Moura da Silveira, M.; Castilho Lopes da Costa, J.P.; Vitolo, M.; Jonas, R.
Activity of glucose-fructose oxidoreductase in fresh and permeabilised cells of Zymomonas mobilis grown in different glucose concentrations
Braz. J. Microbiol.
34
329-333
2003
Zymomonas mobilis
-
Halbig, D.; Wiegert, T.; Blaudeck, N.; Freudl, R.; Sprenger, G.A.
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
Eur. J. Biochem.
263
543-551
1999
Zymomonas mobilis
Lott, J.S.; Halbig, D.; Baker, H.M.; Hardman, M.J.; Sprenger, G.A.; Baker, E.N.
Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation
J. Mol. Biol.
304
575-584
2000
Zymomonas mobilis (Q07982), Zymomonas mobilis
Erzinger, G.S.; Vitolo, M.
Zymomonas mobilis as catalyst for the biotechnological production of sorbitol and gluconic acid
Appl. Biochem. Biotechnol.
129-132
787-794
2006
Zymomonas mobilis
Zhang, X.; Chen, G.; Liu, W.
Reduction of xylose to xylitol catalyzed by glucose-fructose oxidoreductase from Zymomonas mobilis
FEMS Microbiol. Lett.
293
214-219
2009
Zymomonas mobilis (Q07982), Zymomonas mobilis
Peretti, F.; Silveira, M.; Zeni, M.
Use of electrodialysis technique for the separation of lactobionic acid produced by Zymomonas mobilis
Desalination
245
626-630
2009
Zymomonas mobilis, Zymomonas mobilis ATCC 29191
-
Aziz, M.; Yusof, Y.; Kulbe, K.
Production and application of glucose-fructose oxidoreductase for conversion of pineapple juice sugars
Afr. J. Microbiol. Res.
5
5046-5052
2011
Zymomonas mobilis, Zymomonas mobilis DSM 473
-
Malvessi, E.; Carra, S.; da Silveira, M.; Ayub, M.
Effect of substrate concentration, pH, and temperature on the activity of the complex glucose-fructose oxidoreductase/glucono-delta-lactonase present in calcium alginate-immobilized Zymomonas mobilis cells
Biochem. Eng. J.
51
1-6
2010
Zymomonas mobilis, Zymomonas mobilis ATCC 29191
-
Aziz, M.G.; Michlmayr, H.; Kulbe, K.D.; Del Hierro, A.M.
Biotransformation of pineapple juice sugars into dietetic derivatives by using a cell free oxidoreductase from Zymomonas mobilis together with commercial invertase
Enzyme Microb. Technol.
48
85-91
2011
Zymomonas mobilis
Pedruzzi, I.; da Silva, E.A.; Rodrigues, A.E.
Production of lactobionic acid and sorbitol from lactose/fructose substrate using GFOR/GL enzymes from Zymomonas mobilis cells: a kinetic study
Enzyme Microb. Technol.
49
183-191
2011
Zymomonas mobilis, Zymomonas mobilis ATCC 29191
Severo, J.B.; Pinto, J.C.; Ferraz, H.C.; Alves, T.L.
Analysis of experimental errors in bioprocesses. 1. Production of lactobionic acid and sorbitol using the GFOR (glucose-fructose oxidoreductase) enzyme from permeabilized cells of Zymomonas mobilis
J. Ind. Microbiol. Biotechnol.
38
1575-1585
2011
Zymomonas mobilis, Zymomonas mobilis ATCC 31821
Malvessi, E.; Carra, S.; Pasquali, F.C.; Kern, D.B.; da Silveira, M.M.; Ayub, M.A.
Production of organic acids by periplasmic enzymes present in free and immobilized cells of Zymomonas mobilis
J. Ind. Microbiol. Biotechnol.
40
1-10
2013
Zymomonas mobilis, Zymomonas mobilis ATCC 29191
Carra, S.; Rodrigues, D.C.; Beraldo, N.M.C.; Folle, A.B.; Delagustin, M.G.; de Souza, B.C.; Reginatto, C.; Polidoro, T.A.; da Silveira, M.M.; Bassani, V.L.; Malvessi, E.
High lactobionic acid production by immobilized Zymomonas mobilis cells a great step for large-scale process
Bioprocess Biosyst. Eng.
43
1265-1276
2020
Zymomonas mobilis (Q07982), Zymomonas mobilis, Zymomonas mobilis ATCC 29191 (Q07982)
EXTERNAL LINKS (specific for EC-Number 1.1.99.28)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
