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Information on EC 1.1.1.119 - glucose 1-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.119
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.119 glucose 1-dehydrogenase (NADP+)
IUBMB Comments
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.119
-
photorespiration
- megaterium
- synthesis
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photorespiratory
- 2-ketogluconate
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biocatalysis
- analysis
- industry
showSynonyms
glcdh, glucose-1-dehydrogenase, nadp-dependent glucose dehydrogenase, nad(p)-dependent gdh, halophilic glucose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glucose (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
GDH
GlcDH
glucose dehydrogenase
NADP-dependent glucose dehydrogenase
-
-
-
-
NADP-linked aldohexose dehydrogenase
-
-
-
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nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase
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-
-
-
STK_17040
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Entner-Doudoroff pathway II (non-phosphorylative), Entner-Doudoroff pathway III (semi-phosphorylative)
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:NADP+ 1-oxidoreductase
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
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CAS REGISTRY NUMBER
COMMENTARY
37250-50-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxy-D-mannose + NADP+
2-amino-2-deoxy-D-mannono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
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Substrates: -
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: the enzyme has a strong preference for NADP+ over NAD+
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
Substrates: -
Products: -
Products: -
?
D-glucose + polyethylene glycol(MW 20000)-N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + polyethylene glycol(MW 20000)-N6-(2-aminoethyl)-NADPH + H+
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Substrates: -
Products: -
Products: -
r
additional information
?
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-
Substrates: reduction of C=N bonds with good levels of conversion (more than 50%) and excellent enantioselectivity (up to more than 99% enantiomeric excess) by glucose dehydrogenase represents a promiscuous catalytic activity of this enzyme
Products: -
Products: -
?
beta-D-glucose + NAD+
?
Substrates: activity with NAD+ is 26% of the activity with NADP+
Products: -
Products: -
?
beta-D-glucose + NAD+
?
Substrates: activity with NAD+ is 26% of the activity with NADP+
Products: -
Products: -
?
beta-D-glucose + NADP+
?
Substrates: activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
Products: -
Products: -
?
beta-D-glucose + NADP+
?
Substrates: activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: the enzyme has a strong preference for NADP+ over NAD+
Products: -
Products: -
?
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
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Substrates: -
Products: -
Products: -
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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Substrates: 4% of the reverse reaction when assayed with D-glucono-1,5-lactone and NADPH at neutral or weak alkaline pH
Products: -
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r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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Substrates: unphosphorylated glucose as substrate
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80°C. At 25°C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80°C. At 25°C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
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Substrates: -
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
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Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: unphosphorylated glucose as substrate
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
NADP+
the Km value of the wild type enzyme is 11fold lower for NADP+ than for NAD+, indicating that the enzyme has a strong preference for NADP+
NADP+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80°C. At 25°C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
NADP+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Mg2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mg2+ is more effective than Mg2+ or Ni2+
Mn2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+
NaCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Ni2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Ni2+ is more effective than Mg2+ or Mn2+
Zinc
a member of the zinc-containing medium chain polyol dehydrogenase family
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
-
at 40°C, half-life in 0.5 M KCl is 86 h for wild-type, and 114 h for mutant D172K/D216K/D344K, 95 h for mutant D172K, 117 h for mutant D216K, 114 h for mutant D344K. At 25°C, half-life in 0.5 M KCl is 506 h for wild-type, and 613 h for mutant D172K/D216K/D344K, 630 h for mutant D172K, 660 h for mutant D216K, 537 h for mutant D344K
additional information
-
overview: sugars found to be neither substrates nor inhibitors
-
additional information
-
not: iodoacetate, N-ethylmaleimide, p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzate)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
-
triple mutant D172K/D216K/D344K shows its maximum activity in a buffer with 0.50-0.75 M NaCl while the wild type protein has its maximum activity with 1.5 M NaCl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.9
beta-D-glucose
wild type enzyme, using NAD+ as cosubstrate
15
beta-D-glucose
mutant enzyme G206D, using NAD+ as cosubstrate
24
beta-D-glucose
mutant enzyme R207I, using NADP+ as cosubstrate
31.1
beta-D-glucose
wild type enzyme, using NADP+ as cosubstrate
32
beta-D-glucose
mutant enzyme R207I, using NAD+ as cosubstrate
52
beta-D-glucose
mutant enzyme G206D, using NADP+ as cosubstrate
57
beta-D-glucose
mutant enzyme G206D/R207I/R208N, using NAD+ as cosubstrate
80
beta-D-glucose
mutant enzyme G206D/R207I, using NAD+ as cosubstrate
57
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
80
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.047
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
0.9
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000008
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
0.000002
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
0.000012
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
0.000038
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9
-
broad range of optimal activity, in Tris-buffer consistently higher than that in phosphate-buffers
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme, enzyme-based synthesis system for poly(3-hydroxybutyrate)
-
-
brenda
expression in Escherichia coli BL21 (DE3) already heterologously overexpressing P450 BM-3 QM together with glucose facilitator (GLF) from Zymomonas mobilis
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GMDH_GLUOX
Gluconobacter oxydans (strain 621H)
266
0
28678
Swiss-Prot
Mitochondrion (Reliability: 1)
Q96ZY7_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
360
1
40283
TrEMBL
-
GLCDH_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
357
0
39242
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.6 A structure determination of the enzyme using crystals grown under conditions that closely mimic those experienced within the cell of the halophile. The structure is compared with nonhalophilic homologues. Location of bound counterions in the structure. Analysis of protein-solvent interactions to further the understanding of the molecular basis of halophilic adaptation
hanging-drop vapour-diffusion method at 17°C, crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein. For most of the complexes, crystals belonging to space group I222 are obtained using sodium/potassium citrate as a precipitant. For the binary and non-productive ternary complexes with NADPH/Zn, it is necessary to replace the citrate with 2-methyl-2,4-pentanediol. Despite the radical change in conditions, the crystals thus formed are isomorphous
hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP+ grow under these conditions. Crystals of form I diffract to beyond 3.5 A resolution and belong to the hexagonal space group P622, with unit-cell parameters a = b = 89.1, c = 214.6 A, alpha = beta = 90°, gamma = 120°. Crystals of form II diffract to greater than 2.0 A and belong to the orthorhombic space group I222 or I212121, with unit-cell parameters a = 61.8, b = 110.9, c = 151.7 A, alpha = beta = gamma = 90°
the structures of GlcDH in binary complexes with either NADP+/Zn2+ or NADPH/Zn2+, a ternary complex with NADP+/Zn2+/glucose, and a nonproductive ternary complex with NADP+/Zn2+ /gluconolactone are determined from isomorphous crystals, in the presence of zinc (1 mM) and either 5 mM NADP+, by using 1.4-1.6 M sodium citrate as the precipitant (in 100 mM HEPES, pH 7.0, and 2 M NaCl) or 5 mM NADPH, using 67-72% (w/v) 2-methyl-2,4-pentanediol as precipitant (in 100 mM HEPES, pH 7.5, and 2 M NaCl)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D172K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D172K/D216K/D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D216K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D38C
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
G206D
G206D/R207I
G206D/R207I/R208N
R207I
D38C
-
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
-
V254I
additional information
G206D
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+
G206D
the mutant is less efficient with NADP+ than the wild type enzyme, the relation kcat/KNAD+ is 1.6times higher than in the wild type, resulting in an enzyme that prefers NAD+ over NADP+
G206D/R207I
no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested
G206D/R207I
the mutant shows no activity with NADP+, when the coenzyme NAD+ is incubated with this double mutant, it reaches the highest kcat value, between 1.5 and 2times higher than the kcat of the wild type enzyme with NADP+, and between 3 and 4times higher than the kcat of the wild type with NAD+
R207I
less efficient with NAD+ or NADP+ than the wild-type enzyme
R207I
the mutant is less efficient with NADP+ than the wild type enzyme, shows an increase of 48times in Km value with NADP+ when compared with the wild type accompanied by a decrease in kcat, which clearly makes the R207I mutant less efficient in catalysis with NADP+, the R207I substitution also makes the enzyme less efficient with NAD+, with a decrease of 4 times in kcat/Km, this substitution also increases the Km for glucose
V254I
mutant has improved kcat and kcat/Km values at both 25°C and 80°C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
V254I
-
mutant has improved kcat and kcat/Km values at both 25°C and 80°C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
-
additional information
-
Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions
additional information
-
introduction of both, GLF and GlcDH, in P450-overexpressing Escherichia coli should enable the cell to carry out a straightforward intracellular cofactor regeneration driven by externally added glucose. For the generation of recombinant Escherichia coli strains carrying two plasmids, these are transformed successively. Firstly, pZY507glf is transformed into Escherichia coli BL21 (DE3). Subsequently, competent cells are prepared from a positive transformant, and then pETDUETbm-3qm glcdh is transformed.
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization of dilute enzyme solutions, below 0.5 ng/ml, results in significant loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
column chromatography on DEAE-Sephadex A-50 and affinty chromatography by blue-dextran Sepharose 4B
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as recombinant protein in Escherichia coli strain BL21(DE3)
expression in Escherichia coli BL21 (DE3) already heterologously overexpressing P450 BM-3 QM together with glucose facilitator (GLF) from Zymomonas mobilis
-
expression in Escherichia coli, together with a glucose facilitator from Zymomonas mobilis for uptake of unphosphorylated glucose
-
overexpression in Escherichia coli JM109 for use as a cofactor regenerator
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
method for determination of D-glucose- and D-galactose levels in glycoconjugates. The NAD(P)H produced from the enzymatic oxidation of the monosaccharides reacts with a CuSO4-bathocuproinedisulfonic acid reagent to produce a color complex absorbing maximally at 486 nm. With galactose dehydrogenase and glucose dehydrogenase serving as the model enzymes, reaction analysis gives a linear plot from 2.5 to 250 nmol of sugar. Method has been applicated to sugar released by acid hydrolysis from lactose, porcine submaxillary mucin and raffinose was quantified
industry
-
Optimizing whole-cell biocatalysts by integrating a recombinant intracellular NADPH regeneration system through co-expression of a glucose facilitator from Zymomonas mobilis for uptake of unphosphorylated glucose and a NADP+-dependent glucose dehydrogenase from Bacillus megaterium that oxidizes glucose to gluconolactone.
synthesis
synthesis
-
use of enzyme in enzyme-catalyzed synthesis system for poly(3-hydroxybutyrate), enzyme catalyzes regeneration of NADPH, system yields 5.6 mg of poly(3-hydroxybutyrate), in a 5 ml-reaction mixture
synthesis
-
Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions
synthesis
-
glucose dehydrogenase is generally used to regenerate the expensive cofactor NADPH by oxidation of D-glucose to gluconolactone
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Avigad, G.; Alroy, Y.; Englard, S.
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1936-1941
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Gluconobacter cerinus
brenda
Avigad, G.; Englard, S.
Aldohexose dehydrogenase from Gluconobacter cerinus-1
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1975
Gluconobacter cerinus
brenda
Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
Crystallization and characterization of NADP-dependent D-glucose dehydrogenase from Gluconobacter suboxydans
Agric. Biol. Chem.
44
301-308
1980
Gluconobacter oxydans
-
brenda
Buckmann, A.F.; Schmid, R.
A different acceptance of adenine-modified NADP+ by NAD(P)+-dependent glucose dehydrogenase from Bacillus megatherium and strictly NADP+-dependent glucose dehydrogenase from Cryptococcus uniguttulatus
Biotechnol. Appl. Biochem.
14
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1991
Filobasidium uniguttulatum, Priestia megaterium
-
brenda
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
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1998
Priestia megaterium
brenda
Johnsen, U.; Selig, M.; Xavier, K.B.; Santos, H.; Schonheit, P.
Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus
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175
52-61
2001
Halococcus saccharolyticus
brenda
Bonete, M.J.; Pire, C.; Llorca, F.I.; Camacho, M.L.
Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence
FEBS Lett.
383
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1996
Haloferax mediterranei (Q977U7), Haloferax mediterranei, Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Satoh, Y.; Tajima, K.; Tannai, H.; Munekata, M.
Enzyme-catalyzed poly(3-hydroxybutyrate) synthesis from acetate with CoA recycling and NADPH regeneration in vitro
J. Biosci. Bioeng.
95
335-341
2003
Cupriavidus necator
brenda
Esclapez, J.; Britton, K.L.; Baker, P.J.; Fisher, M.; Pire, C.; Ferrer, J.; Bonete, M.J.; Rice, D.W.
Crystallization and preliminary X-ray analysis of binary and ternary complexes of Haloferax mediterranei glucose dehydrogenase
Acta Crystallogr. Sect. F
61
743-746
2005
Haloferax mediterranei, Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Schewe, H.; Kaup, B.A.; Schrader, J.
Improvement of P450(BM-3) whole-cell biocatalysis by integrating heterologous cofactor regeneration combining glucose facilitator and dehydrogenase in E. coli
Appl. Microbiol. Biotechnol.
78
55-65
2008
Priestia megaterium
brenda
Esclapez, J.; Pire, C.; Bautista, V.; Martinez-Espinosa, R.M.; Ferrer, J.; Bonete, M.J.
Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis
FEBS Lett.
581
837-842
2007
Haloferax mediterranei
brenda
Sovic, D.; Lester, L.; Murray, E.; Cohenford, M.
The utilization of bathocuproinedisulfonic acid as a reagent for determining D-glucose and D-galactose levels in glycoconjugates
Bioorg. Chem.
36
91-95
2008
Pseudomonas fluorescens
brenda
Pire, C.; Esclapez, J.; Diaz, S.; Perez-Pomares, F.; Ferrer, J.; Bonete, M.
Alteration of coenzyme specificity in halophilic NAD(P)+ glucose dehydrogenase by site-directed mutagenesis
J. Mol. Catal. B
59
261-265
2009
Haloferax mediterranei, Haloferax mediterranei (Q977U7)
-
brenda
Baker, P.J.; Britton, K.L.; Fisher, M.; Esclapez, J.; Pire, C.; Bonete, M.J.; Ferrer, J.; Rice, D.W.
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily
Proc. Natl. Acad. Sci. USA
106
779-784
2009
Haloferax mediterranei (Q977U7)
brenda
Ferrer, J.; Fisher, M.; Burke, J.; Sedelnikova, S.E.; Baker, P.J.; Gilmour, D.J.; Bonete, M.J.; Pire, C.; Esclapez, J.; Rice, D.W.
Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. D
57
1887-1889
2001
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Sugii, T.; Akanuma, S.; Yagi S.; Yagyu, K.; Shimoda, Y.; Yamagishi, A.
Characterization of the low-temperature activity of Sulfolobus tokodaii glucose-1-dehydrogenase mutants
J. Biosci. Bioeng.
118
367-371
2014
Sulfurisphaera tokodaii (Q96ZY7), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q96ZY7)
brenda
Britton, K.L.; Baker, P.J.; Fisher, M.; Ruzheinikov, S.; Gilmour, D.J.; Bonete, M.J.; Ferrer, J.; Pire, C.; Esclapez, J.; Rice, D.W.
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Roth, S.; Praeg, A.; Wechsler, C.; Marolt, M.; Ferlaino, S.; Luedeke, S.; Sandon, N.; Wetzl, D.; Iding, H.; Wirz, B.; Mueller, M.
Extended catalytic scope of a well-known enzyme asymmetric reduction of iminium substrates by glucose dehydrogenase
ChemBioChem
18
1703-1706
2017
Bacillus subtilis
brenda
Hyskova, V.; Pliskova, V.; Cerveny, V.; Ryslava, H.
NADP-dependent enzymes are involved in response to salt and hypoosmotic stress in cucumber plants
Gen. Physiol. Biophys.
36
247-258
2017
Cucumis sativus
brenda
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