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Information on EC 1.1.1.360 - glucose/galactose 1-dehydrogenase
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1.1.1.360 glucose/galactose 1-dehydrogenaseIUBMB Comments
A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)).
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
dual-specific glucose/galactose dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dual-specific glucose/galactose dehydrogenase
GdhA
GlcDH
glucose (galactose) dehydrogenase
TvGlcD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
(2)
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
(2)
-
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
-
-
-
-
D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-glucose/D-galactose 1-dehydrogenase (NADPH)
A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
?
D-galactose + NADP+
?
the activity towards D-galactose is 58% of that observed towards D-glucose
-
?
D-galactose + NADP+
?
the activity towards D-galactose is 58% of that observed towards D-glucose
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
74% of the activity with D-glucose + NADP+
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
74% of the activity with D-glucose + NADP+
-
?
D-glucopyranose + NADP+
D-glucono-1,5-lactone + NADPH + H+
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-glucopyranose + NADP+
D-glucono-1,5-lactone + NADPH + H+
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
?
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
?
additional information
?
-
none of the C2 and C3 epimers of D-glucose or derivatives (D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, glucose-6-phosphate) and none of the aldopentoses (D-xylose, L-arabinose, D-ribose) tested shows activity above 2% both with NADP+ and NAD+ as cosubstrates
-
?
additional information
?
-
-
none of the C2 and C3 epimers of D-glucose or derivatives (D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, glucose-6-phosphate) and none of the aldopentoses (D-xylose, L-arabinose, D-ribose) tested shows activity above 2% both with NADP+ and NAD+ as cosubstrates
-
?
additional information
?
-
none of the C2 and C3 epimers of D-glucose or derivatives (D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, glucose-6-phosphate) and none of the aldopentoses (D-xylose, L-arabinose, D-ribose) tested shows activity above 2% both with NADP+ and NAD+ as cosubstrates
-
?
additional information
?
-
the enzyme does not utilize aldopentoses such as D-xylose
-
?
additional information
?
-
the enzyme does not utilize D-xylose , L-arabinose, D-ribose, D-fructose, and D-mannose as substrates
-
?
additional information
?
-
the enzyme does not utilize aldopentoses such as D-xylose
-
?
additional information
?
-
the enzyme does not utilize D-xylose , L-arabinose, D-ribose, D-fructose, and D-mannose as substrates
-
?
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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-galactose + NADP+
?
the activity towards D-galactose is 58% of that observed towards D-glucose
-
-
?
D-galactose + NADP+
?
the activity towards D-galactose is 58% of that observed towards D-glucose
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
NAD+
the enzyme utilizes NAD+ as a cofactor with nearly the same substrate specificity as NADP, but the electron-acceptor activity of NAD+ (2 mM) is only 4% of that observed with NADP+ (at 100 mM D-glucose)
NADP+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
NADP+
the electron-acceptor activity of NAD+ (2 mM) is only 4% of that observed with NADP+ (at 100 mM D-glucose)
NADP+
the enzyme utilizes NAD+ as a cofactor with nearly the same substrate specificity as NADP, but the electron-acceptor activity of NAD+ (2 mM) is only 4% of that observed with NADP+ (at 100 mM D-glucose)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the enzyme contains structurally important zinc, the enzyme also contains Zn2+ near the catalytic site. Addition of ZnCl2 to the assay buffer at up to 5 mM has no effect on activity
additional information
additional information
addition of 5 mM NaCl, MgCl2, MnCl2 or CaCl2 has no effect
additional information
-
addition of 5 mM NaCl, MgCl2, MnCl2 or CaCl2 has no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
inhibition displays Michaelis-Menten kinetics in a noncompetitive mode with respect to the cofactor NADP+
additional information
EDTA added at up to 10 mm causes no loss of activity. Pyruvate, phosphoenolpyruvate, 3-phosphoglycerate, 2-phosphoglycerate, phosphate and diphosphate do not affect the activity when added to the standard assay at 5 or 20 mm
-
additional information
-
EDTA added at up to 10 mm causes no loss of activity. Pyruvate, phosphoenolpyruvate, 3-phosphoglycerate, 2-phosphoglycerate, phosphate and diphosphate do not affect the activity when added to the standard assay at 5 or 20 mm
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
NADP+
pH 6.5, 55°C, wild-type enzyme or mutant enzyme T277F
additional information
NAD+
the precise determination of the Km for NAD+ is not possible, as it is impossible to reach saturation of the enzyme
additional information
NAD+
-
the precise determination of the Km for NAD+ is not possible, as it is impossible to reach saturation of the enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
ATP
pH 6.5, 55°C, at saturating glucose concentration (50 mM)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
356
498
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the Entner–Doudoroff pathway
physiological function
-
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the Entner–Doudoroff pathway
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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). GLCD2_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
359
0
40463
Swiss-Prot
-
Q979W2_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
361
0
40246
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of substrate/cofactor-free tvGlcDH and of a tvGlcDH T277F mutant in a binary complex with NADP and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, an NADP analogue, are determined at resolutions of 2.6, 2.25 and 2.33 A
in a binary complex with NADP+ and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, sitting drop vapor diffusion method, using 30% (w/v) 1,2-propanediol, 20% (w/v) polyethylene glycol 400 (PEG 400), 0.1 M HEPES pH 7.5
ultrafiltration, sitting-drop vapour-diffusion method, crystal structures of substrate/cofactor-free enzyme and of a T277F mutant enzyme in a binary complex with NADP+ and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, an NADP+ analogue, are determined at resolutions of 2.6, 2.25 and 2.33 A, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D306N
E156Q
E296H
K159A
K159A/N160D
N160D
T277F
V93N
V93N/D306N
V93N/E156Q/K159A/N160D/D306N/E296H
V93N/K159A
V93N/K159A/N160D
V93N/N160D
D306N
-
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
K159A
N160D
D306N
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
D306N
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
E156Q
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
E156Q
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
E296H
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
E296H
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
K159A
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
K159A
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
K159A/N160D
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
K159A/N160D
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
N160D
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
N160D
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
T277F
crystal structure of the T277F mutant enzyme in a binary complex with NADP+ and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate. The Vmax for the T277F mutant is about 12% of that for the wild-type enzyme
T277F
crystallization of the T277F mutant enzyme in a binary complex with NADP and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, mutation reduces the D-glucose oxidation activity, the Vmax for the T277F mutant is about 12% of that for the wild-type enzyme
V93N
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
V93N
the Vmax value for D-glucose oxidation by the purified V93N mutant is about 71% of the Vmax value for the wild-type enzyme. Enhancement of the activity towards D-xylose is not observed
V93N/D306N
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
V93N/D306N
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
V93N/E156Q/K159A/N160D/D306N/E296H
activity is completely abolished
V93N/E156Q/K159A/N160D/D306N/E296H
mutation completely abolished the activity of the enzyme
V93N/K159A
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
V93N/K159A
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
V93N/K159A/N160D
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
V93N/K159A/N160D
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
V93N/N160D
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
V93N/N160D
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
K159A
-
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
K159A
-
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
N160D
-
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
N160D
-
improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6 - 9
the enzyme loses no activity when incubated at pH values between 6.0 and 9.0 for 10 min at 40°C
726594
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
the enzyme retains more than 90% of its activity after incubation for 10 min at temperatures of up to 40°C
60
70
pH 6.5, without the addition of Zn2+, t1/2: 5 min. At 1 mM Zn2+ the enzyme is stable for 3 h
additional information
additional information
Zn2+ improves thermal stability. EDTA completely abolishes the stabilizing effect of Zn2+
additional information
-
Zn2+ improves thermal stability. EDTA completely abolishes the stabilizing effect of Zn2+
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Ethanol
Methanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-charged chelating Sepharose column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Angelov, A.; Fuetterer, O.; Valerius, O.; Braus, G.H.; Liebl, W.
Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus
FEBS J.
272
1054-1062
2005
Picrophilus torridus (Q6L047), Picrophilus torridus, Picrophilus torridus DSM 9790 (Q6L047)
brenda
Kanoh, Y.; Uehara, S.; Iwata, H.; Yoneda, K.; Ohshima, T.; Sakuraba, H.
Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium
Acta Crystallogr. Sect. D
70
1271-1280
2014
Thermoplasma volcanium (Q979W2), Thermoplasma volcanium DSM 4299 (Q979W2)
brenda
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