Information on EC 1.1.1.360 - glucose/galactose 1-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.360
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RECOMMENDED NAME
GeneOntology No.
glucose/galactose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Entner-Doudoroff pathway II (non-phosphorylative)
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Entner-Doudoroff pathway III (semi-phosphorylative)
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Galactose metabolism
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Pentose phosphate pathway
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Entner Doudoroff pathway
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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+)).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the Entner–Doudoroff pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactopyranose + NADP+
D-galactono-1,5-lactone + NADPH + H+
show the reaction diagram
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
show the reaction diagram
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
show the reaction diagram
D-glucopyranose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
show the reaction diagram
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetone
20% (v/v), 40% loss of activity
ATP
inhibition displays Michaelis-Menten kinetics in a noncompetitive mode with respect to the cofactor NADP+
ethanol
20% (v/v), 20% loss of activity
methanol
20% (v/v), 30% loss of activity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.7
D-galactopyranose
pH 6.5, 55°C, wild-type enzyme
4.5
D-galactose
pH 6.5, 55°C, cosubstrate: NADP+
7.1
D-glucopyranose
pH 6.5, 55°C, wild-type enzyme
10
D-glucose
pH 6.5, 55°C, cosubstrate: NADP+
0.14 - 1.12
NADP+
additional information
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9
ATP
pH 6.5, 55°C, at saturating glucose concentration (50 mM)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
pH 6.5, 55°C, D-glucose oxidation, T277F mutant
252
pH 6.5, 55°C, NADP+ (cosubstrate: D-glucose)
356
pH 6.5, 55°C, D-glucose oxidation, V93N mutant; pH 6.5, 55°C, mutant enzyme V93N
498
pH 6.5, 55°C, D-glucose oxidation, wild-type enzyme; pH 6.5, 55°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
55°C: optimum, 60°C: 88% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40462
4 * 40462, calculated from sequence
40500
4 * 40500, SDS-PAGE
41311
4 * 41311, calculated from sequence
42000
4 * 42000, SDS-PAGE
158000
gel filtration
160000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
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; 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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
10 min, at 60°C, no loss of activity; 60°C, 10 min, stable
726594
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
10 min, retains more than 90% of its activity; 10 min, the enzyme retains more than 90% of its activity
65
pH 6.5, without the addition of Zn2+, t1/2: 3 h
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
Ethanol
Methanol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D306N
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity; 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; 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; 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; 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; 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; improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
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; 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
V93N
enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity; 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; 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; 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; 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; 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; improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
D306N
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enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity
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K159A
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enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity; improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
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N160D
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enhancement of the activity towards D-xylose is not observed, mutation reduces the D-glucose oxidation activity; improvement of the reactivity towards D-xylose can not be achieved, while the mutations reduces the D-glucose oxidation activity
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