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Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+] and Organism(s) Priestia megaterium and UniProt Accession P39485

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EC Tree
IUBMB Comments
This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
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This record set is specific for:
Priestia megaterium
UNIPROT: P39485
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Word Map
The taxonomic range for the selected organisms is: Priestia megaterium
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
hexose-6-phosphate dehydrogenase, glcdh-i, glcdh-ii, ssgdh, glcdh-iwg3, bmglcdh-iv, lsgdh, bzgdh, hexose phosphate dehydrogenase, nad(p)-dependent glucose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucose 1-dehydrogenase IV
-
beta-D-glucose:NAD(P)+ 1-oxido-reductase
-
-
beta-D-glucose:NAD(P)+ 1-oxidoreductase
-
-
-
-
BmGlcDH-III
-
-
D-glucose dehydrogenase (NAD(P))
-
-
-
-
general stress protein 74
-
-
-
-
GlcDH
GlcDH-I
isozyme is unstable throughout pH range 4-10
GlcDH-II
-
isozyme is stable in the alkaline pH region
GlcDH-IWG3
isozyme is stable in the acidic pH region
glucose 1-dehydrogenase III
-
-
glucose dehydrogenase
GSP74
-
-
-
-
hexose phosphate dehydrogenase
-
-
-
-
hexose-6-phosphate dehydrogenase
-
-
-
-
additional information
-
enzyme belongs to the family of short-chain dehydrogenases/reductases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucose:NAD(P)+ 1-oxidoreductase
This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-53-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 9.1% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 11% (reference: D-glucose 100%)
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 18% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 35% (reference: D-glucose 100%)
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
14% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
2-deoxy-D-glucose + NAD+
?
show the reaction diagram
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
-
best substrate, wild-type and mutant enzymes
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-fructose + NAD(P)+
? + NAD(P)H
show the reaction diagram
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-fructose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
show the reaction diagram
-
low activity with wild-type and mutant enzymes
-
-
?
D-galactose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 2.9% (reference: D-glucose 100%)
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
-
?
D-glucosamine + NAD+
?
show the reaction diagram
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
show the reaction diagram
-
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 3% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NADP+
D-glucosamino-1,5-lactone + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
show the reaction diagram
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
75% relative activity
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
show the reaction diagram
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
show the reaction diagram
-
wild-type and mutant enzymes
-
-
?
D-mannose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
show the reaction diagram
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 4.8% (reference: D-glucose 100%)
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
-
wild-type and mutant enzymes
-
-
?
D-xylose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
show the reaction diagram
substrate specificity wild-tpye: 10% (reference: D-glucose 100%)
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
stabilizes the enzyme at alkline pH and elevated temperatures
additional information
-
does not require Zn2+ for enzymatic action
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(2-bromoacetyl)pyridine
active-site-directed irreverseible inhibitor, the cofactor NAD but not the substrate glucose protects the enzyme from the inactivation, in the presence of 0.1 M NAD and 1.37 mM 3-(2-bromoacetyl)pyridine, glucose dehydrogenase has still 85% of its original activity after incubation for 2 h
NaCl
-
reaction rate and dissociation at pH 9 are reduced by increasing the NaCl concentration (0-500 mM)
Tetranitromethane
the rapid inactivation can be prevented by the presence of NAD, AMP, or ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1 - 5000
D-glucose
2.7 - 135
beta-D-glucose
7.5 - 63
D-glucose
0.018 - 7
NAD+
0.0051 - 18.9
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18 - 802
beta-D-glucose
81.9 - 395
D-glucose
23 - 390
NAD+
18 - 300
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.7 - 6.9
D-glucose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
3-(2-bromoacetyl)pyridine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
169
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
227
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
239
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
acetate/borate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sharp drop in activity at alkaline pH of wild-type and mutant Q252L activities, not mutant Q252L/E170K
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 4.8
-
isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHG4_PRIMG
261
0
28157
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112800
gel filtration
116000
-
gel filtration
120000
150000
GlcDH-II, gel filtration
28090
subunit, calculated from amino acid sequence
28200
29000
30000
34000
-
x * 34000, GlcDH-II and GlcDH-IV, SDS-PAGE
36000
-
x * 36000, enzyme form GlcDH-II, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structures of BmGlcDH-IV in ligand-free, NADH-bound and beta-D-glucose-bound forms is determined to a resolution of 2.0 A
1.7 A resoluton, four subunits are interrelated by three mutually perpendicular diad axes P,Q and R
batch method using ammonium sulfate as precipitant at pH 6.5 and microdialysis technique with 60% ammonium sulfate in 334 mM NAD, pH 5.8-6.8
-
hanging drop vapour diffusion method with 28% (w/v) PEG 2000, 4 mM NAD+, 40 mM sodium phosphate pH 6.0
micro-seedingtechnique using PEG 2000 as a precipitant
the crystal structures of BmGlcDH-IV in ligand-free, NADH-bound and beta-D-glucose-bound forms is determined to a resolution of 2.0 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A258F
Km (D-glucose) increased at pH 6 compared to wild-type, decreased at pH 8 compared to wild-type. Mutant shows higher substrate specificity with D-xylose, D-mannose, D-galactose and D-glucosamine compared to wild-type. Mutant shows a markedly deteriorated thermostability
DELTAG261
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type.Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Mutant shows a markedly deteriorated thermostability
G259A
Km (D-glucose) increased at pH 6 and pH 8 compared to wild-type. Specific activity of the G259A mutant is slightly lower, but is still comparable with wild-type BmGlcDH-IV. Thermostability comparable to wild-type
G259V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261A
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
E170K
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
E96K
-
mutation increases thermostability by about 15°C at pH 6.5
E96K/D108N/P194Q/E210K
mutant enzyme has higher stability at 60°C and 97% remaining activity compared to the wild type enzyme
E96K/V112A/E133K/Y217H
mutant enzyme has higher stability at 60°C and 85% remaining activity compared to the wild type enzyme
E96K/V183I
mutant enzyme has higher stability at 60°C and 72% remaining activity compared to the wild type enzyme
Q252L
Q252L/A258G
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K
Q252L/E170K/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/K137R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I/K137R
the mutant enzyme exhibits a 9.2fold increase in tolerance against 10% (v/v) 1-phenylethanol and is more stable than mutant enzyme Q252L/E170K (BmGDHM0) when exposed to hydrophobic and enzyme-inactivating compounds such as acetophenone, ethyl 2-oxo-4-phenylbutyrate, and ethyl (R)-2-hydroxy-4-phenylbutyrate
Y253C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
30 min, about 50% loss of activity
639125
4 - 10
-
30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity
639105
4 - 8
-
30°C, 20 min, mutant enzyme Q252L is stable
639105
5
-
30°C, 20 min, about 55% loss of activity of mutant enzyme Y253C, about 35% loss of activity of mutant enzyme E96G and wild-type enzyme
639105
5 - 10
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-III is stable
639101
5 - 6.5
-
30 min, stable
639125
5.5 - 10
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-V is stable
639101
6 - 7
-
30°C, 20 min, wild-type and mutant enzyme Y253C are stable
639105
6 - 9
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-IWG3 is stable
639101
6.5 - 7
-
20 min, without NaCl, isoenzyme GlcDH-IWG3 and GlcDH-III are stable
639101
6.5 - 9
-
the enzyme is stable and active at pH 6.5, by shifting the pH to 9.0 the enzyme is completely and irreversibly dissociated into four inactive protomers
639108
7 - 9
wild type GlcDH shows reversible dissociation-association between inactive monomers and active tetramers when the pH is shifted between 9 and 7
677657
7.3
-
30 min, about 50% loss of activity
639125
7.5
-
30 min, about 95% loss of activity
639125
8
-
30°C, 20 min, about 50% loss of activity of mutant enzyme Y253C, about 80% loss of wild-type enzyme, about 30% loss of activity of mutant enzyme E96G and E96, about 15% loss of activity of mutant enzyme E96K
639105
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
wild-type enzyme retains 70% activity after 40 min at 65°C
30
-
20 min, isoenzyme GlcDH-III, without NaCl, about 55% loss of activity
40
-
pH 6.5, 20 min, wild-type enzyme is stable
45
-
20 min, isoenzyme GlcDH-IV, without NaCl, about 35% loss of activity, isoenzyme IWG3, without NaCl, about 10% loss of activity
55
-
pH 6.5, 20 min, about 65% loss of acticity of mutant enzyme Y253C, about 20% loss of activity of mutant enzyme Y252L, mutant enzyme E96K, E96G and E96A are stable
60
-
pH 6.5, 20 min, complete loss of activity of enzyme Y253C about 95% loss of activity of mutant enzyme Y252L, about 30% loss of activity of mutant enzyme E96G, mutant enzymes E96K and E95A are stable
66
-
half-life: mutant Q252L 1.3 min, mutant Q252L/E170K 540 min
70
-
20 min, presence of 2 mM NaCl, complete inactivation of isoenzyme GlcDH-III and GlcDH-IV, isoenzyme GlcDH-IWG3 loses 30% of initial activity
additional information
-
thermostability is highly increased by addition of NaCl
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glucose dehydrogenase isoenzymes are stabilized in presence of 2 M NaCl. The effect is especially large for GlcDH-III, which is the most unstable enzyme
-
NaCl stabilizes the enzyme at alkline pH and elevated temperatures
-
purified enzyme is indefinitely stable in the frozen state or in solution at pH 6.5 containing 3 M NaCl and a protein concentration of more than 0.5 mg/ml. Diluted enzyme solutions can be stabilized to the same degree by adding 0.5% polyvinylpyrrolidone. Any reduction of the ionic strength of enzyme solution leads to an irreversible inactivation which can be only partially prevented by additrion of polyvinylpyrrolidone
-
unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl
-
unstable at low ionic strength, in 67 mM phosphate buffer enzyme activity decreases to 80% within 5 hours at pH 6.5 and 0.01 mg/ml protein, reduction to 57% at 40 mM phosphate, high concentration of NAD inhibit dissociation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phenylethanol
mutant enzymes Q252L/E170K/S100P and Q252L/E170K/K166R display a 2.9fold and 2.0fold improvement in tolerance against 1-phenylethanol, respectively, compared with mutant enzyme Q252L/E170K. The half-life (t1/2) of mutant enzyme Q252L/E170K/S100P/K166R in the presence of 10% (v/v) 1-phenylethanol is prolonged from 70.4 min to 319 min, representing a 4.5fold increase compared with mutant enzyme Q252L/E170K. The chemical tolerance of mutant enzyme Q252L/E170K/S100P/K166R/V72I and mutant enzyme Q252L/E170K/S100P/K166R/K137R against 10% (v/v) 1-phenylethanol is increased by 5.6fold and 6.7fold, respectively, compared with mutant enzyme Q252L/E170K
acetophenone
mutant enzyme Q252L/E170K retains 8% of initial activity when incubated for 12 h with 10% acetophenone
DMSO
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) DMSO
Methanol
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) metanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM sodium phosphate pH 6.5, 2 M NaCl, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephadex A-50 gel filtration
DEAE-Sepharose CL-6B column chromatography
high-pressure liquid chromatography
hydroxyapatite, QAE-Sephadex
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
Sephadex G-100 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein
DNA sequence determination and analysis, expression in Escherichia coli strain JM109
-
E96K mutant enzyme
-
expressed as a His-tagged fusion protein
expressed in Escherichia coli
expressed in Escherichia coli KP3998 cells
expressed in Escherichia coli strain JM109
expressed in Escherichia coli strain JM109 (pGDA2)
expressed in Escherichia coli, isoenzymes III and IV
-
expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3) with a combined lac and T7 promoter
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation of enzyme denatured by urea, restores more than 90% of the original activity 60 min after dilution and after complete dialysis. Optimal temperature for refolding is 25°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
-
co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes
diagnostics
-
usage for quantitative determination of glucose in clinical tests and in the food industry
energy production
-
NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kataoka, M.; Rohani, L.P.S.; Wada, M.; Kita, K.; Yanase, H.; Urabe, I.; Shimizu, S.
Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system
Biosci. Biotechnol. Biochem.
62
167-169
1998
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Yamamoto, K.; Kurisi, G.; Kusunoki, M.; Tabata, S.; Urabe, I.; Osaki, S.
Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution
J. Biochem.
129
303-312
2001
Priestia megaterium, Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Nagao, T.; Mitamura, T.; Wang, X.H.; Negoro, S.; Yomo, T.; Urabe, I.; Okada, H.
Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isoenzymes from Bacillus megaterium IAM1030
J. Bacteriol.
174
5013-5020
1992
Priestia megaterium
Manually annotated by BRENDA team
Yamamot, K.; Nagao, T.; Makino, Y.; Urabe, I.; Okada, H.
Characterization of mutant glucose dehydrogenase with increasing stability
Ann. N. Y. Acad. Sci.
613
362-365
1990
Priestia megaterium
Manually annotated by BRENDA team
Maurer, e.; Pfleiderer, G.
Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. II. Kinetics and mechanism
Z. Naturforsch. C
42
907-915
1987
Priestia megaterium
Manually annotated by BRENDA team
Hnes, J.; Jany, K.D.; Pfleiderer, G.; Wagner, A.F.V.
An integrated prediction of secondary, tertiary and quarternary structure of glucose dehydrogenase
FEBS Lett.
212
193-198
1987
Priestia megaterium
Manually annotated by BRENDA team
Maurer, E.; Pfleiderer, G.
Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. I. Conformational and functional changes
Biochim. Biophys. Acta
827
381-388
1985
Priestia megaterium
-
Manually annotated by BRENDA team
Pauly, H.E.; Pfleiderer, G.
Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenase
Biochemistry
16
4599-4604
1977
Priestia megaterium
Manually annotated by BRENDA team
Pauly, H.E.; Pfleiderer, G.
D-Glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure
Hoppe-Seyler's Z. Physiol. Chem.
356
1613-1623
1975
Priestia megaterium
Manually annotated by BRENDA team
Baik, S.H.; Ide, T.; Yoshida, H.; Kagami, O.; Harayama, S.
Significantly enhanced stability of glucose dehydrogenase by directed evolution
Appl. Microbiol. Biotechnol.
61
329-335
2003
Bacillus licheniformis, Bacillus subtilis, Priestia megaterium
Manually annotated by BRENDA team
Yamamoto, K.; Kusunoki, M.; Urabe, I.; Tabata, S.; Osaki, S.
Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Bacillus megaterium IWG3
Acta Crystallogr. Sect. D
56
1443-1445
2000
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Baik, S.H.; Michel, F.; Aghajari, N.; Haser, R.; Harayama, S.
Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state
Appl. Environ. Microbiol.
71
3285-3293
2005
Priestia megaterium (P40288), Priestia megaterium IGW3 (P40288)
Manually annotated by BRENDA team
Ulmer, W.; Froeschle, M.; Jany, K.D.
Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine
Eur. J. Biochem.
136
183-194
1983
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Froeschle, M.; Ulmer, W.; Jany, K.D.
Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state
Eur. J. Biochem.
142
533-540
1984
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Pal, G.P.; Jany, K.D.; Saenger, W.
Crystallization of and X-ray investigations on glucose dehydrogenase from Bacillus megaterium
Eur. J. Biochem.
167
123-124
1987
Priestia megaterium, Priestia megaterium MI286
Manually annotated by BRENDA team
Heilmann, H.J.; Maegert, H.J.; Gassen, H.G.
Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli
Eur. J. Biochem.
174
485-490
1988
Priestia megaterium, Priestia megaterium M1286
Manually annotated by BRENDA team
Mitamura, T.; Urabe, I.; Okada, H.
Enzymatic properties of isozymes and variants of glucose dehydrogenase from Bacillus megaterium
Eur. J. Biochem.
186
389-393
1989
Priestia megaterium, Priestia megaterium (P39482), Priestia megaterium (P40288), Priestia megaterium IAM 1030, Priestia megaterium IAM 1030 (P39482), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Makino, Y.; Negoro, S.; Urabe, I.; Okada, H.
Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3
J. Biol. Chem.
264
6381-6385
1989
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Muratsubaki, H.; Enomoto, K.; Soejima, A.; Satake, K.
An enzyme cycling method for measurement of allantoin in human serum
Anal. Biochem.
378
65-70
2008
Priestia megaterium
Manually annotated by BRENDA team
Xu, Z.; Jing, K.; Liu, Y.; Cen, P.
High-level expression of recombinant glucose dehydrogenase and its application in NADPH regeneration
J. Ind. Microbiol. Biotechnol.
34
83-90
2007
Priestia megaterium, Priestia megaterium AS1.223
Manually annotated by BRENDA team
Nishioka, T.; Yasutake, Y.; Nishiya, Y.; Tamura, T.
Structure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1-dehydrogenase IV
FEBS J.
279
3264-3275
2012
Priestia megaterium, Priestia megaterium (P39485)
Manually annotated by BRENDA team
Stolarczyk, K.; Rogalski, J.; Bilewicz, R.
NAD(P)-dependent glucose dehydrogenase applications for biosensors, bioelectrodes, and biofuel cells
Bioelectrochemistry
135
107574
2020
Aspergillus niger, Priestia megaterium, Thermoplasma acidophilum
-
Manually annotated by BRENDA team
Qian, W.; Ou, L.; Li, C.; Pan, J.; Xu, J.; Chen, Q.; Zheng, G.
Evolution of glucose dehydrogenase for cofactor regeneration in bioredox processes with denaturing agents
ChemBioChem
21
2680-2688
2020
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
Manually annotated by BRENDA team
Plz, M.; Petrovicova, T.; Rebros, M.
Semi-continuous flow biocatalysis with affinity co-immobilized ketoreductase and glucose dehydrogenase
Molecules
25
4278
2020
Priestia megaterium
Manually annotated by BRENDA team