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Information on EC 1.1.1.360 - glucose/galactose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.360
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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
1.1.1.360 glucose/galactose 1-dehydrogenase
IUBMB 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+)).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
showSynonyms
dual-specific glucose/galactose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dual-specific glucose/galactose dehydrogenase
GdhA
GlcDH
glucose (galactose) dehydrogenase
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
MetaCyc
Entner-Doudoroff pathway II (non-phosphorylative), Entner-Doudoroff pathway III (semi-phosphorylative)
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + NADP+
D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
Substrates: prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
Substrates: prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the activity towards D-galactose is 58% of that observed towards D-glucose
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the activity towards D-galactose is 58% of that observed towards D-glucose
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
Substrates: 74% of the activity with D-glucose + NADP+
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
Substrates: 74% of the activity with D-glucose + NADP+
Products: -
Products: -
?
D-glucopyranose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-glucopyranose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Products: -
Products: -
?
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Products: -
Products: -
?
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not utilize aldopentoses such as D-xylose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not utilize D-xylose , L-arabinose, D-ribose, D-fructose, and D-mannose as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not utilize aldopentoses such as D-xylose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not utilize D-xylose , L-arabinose, D-ribose, D-fructose, and D-mannose as 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-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the activity towards D-galactose is 58% of that observed towards D-glucose
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the activity towards D-galactose is 58% of that observed towards D-glucose
Products: -
Products: -
?
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the EntnerDoudoroff pathway
physiological function
-
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the EntnerDoudoroff 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
EXTERNAL LINKS (specific for EC-Number 1.1.1.360)
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