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Information on EC 1.1.1.119 - glucose 1-dehydrogenase (NADP+)
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EC Tree
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.
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Word Map
- 1.1.1.119
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photorespiration
- megaterium
- synthesis
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photorespiratory
- 2-ketogluconate
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biocatalysis
- analysis
- industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glcdh, glucose-1-dehydrogenase, nadp-dependent glucose dehydrogenase, nad(p)-dependent gdh, halophilic glucose dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glucose (nicotinamide adenine dinucleotide phosphate)
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GDH
GlcDH
glucose dehydrogenase
NADP-dependent glucose dehydrogenase
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NADP-linked aldohexose dehydrogenase
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nicotinamide adenine dinucleotide (phosphate)-dependent glucose-1-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
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
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
2-amino-2-deoxy-D-mannose + NADP+
2-amino-2-deoxy-D-mannono-1,5-lactone + NADPH
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?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
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?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
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?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
the enzyme has a strong preference for NADP+ over NAD+
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?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
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?
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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r
additional information
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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
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beta-D-glucose + NAD+
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activity with NAD+ is 26% of the activity with NADP+
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beta-D-glucose + NAD+
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activity with NAD+ is 26% of the activity with NADP+
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?
beta-D-glucose + NADP+
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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+)
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?
beta-D-glucose + NADP+
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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+)
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?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme has a strong preference for NADP+ over NAD+
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?
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
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r
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
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r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
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r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
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r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
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r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
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r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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4% of the reverse reaction when assayed with D-glucono-1,5-lactone and NADPH at neutral or weak alkaline pH
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r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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unphosphorylated glucose as substrate
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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+
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D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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+
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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 + NADP+
D-glucono-1,5-lactone + NADPH + H+
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unphosphorylated glucose as substrate
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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?
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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+
Km-value for NAD+ is 50fold higher than Km-value 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+
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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
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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
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overview: sugars found to be neither substrates nor inhibitors
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additional information
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not: iodoacetate, N-ethylmaleimide, p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzate)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
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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
0.0293
D-glucose
mutant enzyme I189V, at pH 9.0 and 25°C
0.0391
D-glucose
mutant enzyme V254I, at pH 9.0 and 25°C
0.314
D-glucose
mutant enzyme I189V, at pH 9.0 and 80°C
0.457
D-glucose
mutant enzyme V254I, at pH 9.0 and 80°C
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
0.0097
D-glucose
mutant enzyme I189V, at pH 9.0 and 80°C
0.0167
D-glucose
mutant enzyme V254I, at pH 9.0 and 80°C
0.047
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
0.085
D-glucose
mutant enzyme I189V, at pH 9.0 and 25°C
0.205
D-glucose
mutant enzyme V254I, at pH 9.0 and 25°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