Information on EC 1.1.1.360 - glucose/galactose 1-dehydrogenase

for references in articles please use BRENDA:EC1.1.1.360
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.360
-
RECOMMENDED NAME
GeneOntology No.
glucose/galactose 1-dehydrogenase
-
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
Entner-Doudoroff pathway II (non-phosphorylative)
-
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
-
Entner Doudoroff pathway
-
-
Pentose phosphate pathway
-
-
Galactose metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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 EntnerDoudoroff 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+
?
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+
D-gluconate + NADPH + H+
show the reaction diagram
-
-
-
?
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-galactose + NADP+
?
show the reaction diagram
D-glucose + NADP+
D-gluconate + NADPH + H+
show the reaction diagram
Q979W2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.7
D-galactopyranose
pH 6.5, 55C, wild-type enzyme
4.5 - 8.7
D-galactose
7.1
D-glucopyranose
pH 6.5, 55C, wild-type enzyme
7.1 - 10
D-glucose
0.14 - 1.12
NADP+
additional information
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9
ATP
pH 6.5, 55C, at saturating glucose concentration (50 mM)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
pH 6.5, 55C, D-glucose oxidation, T277F mutant
252
pH 6.5, 55C, NADP+ (cosubstrate: D-glucose)
356
pH 6.5, 55C, D-glucose oxidation, V93N mutant; pH 6.5, 55C, mutant enzyme V93N
498
pH 6.5, 55C, D-glucose oxidation, wild-type enzyme; pH 6.5, 55C, 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
55C: optimum, 60C: 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; 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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
10 min, at 60C, no loss of activity; 60C, 10 min, stable; the enzyme loses no activity when incubated at pH values between 6.0 and 9.0 for 10 min at 40C
726594
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
the enzyme retains more than 90% of its activity after incubation for 10 min at temperatures of up to 40C
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
; nickel-charged chelating Sepharose column chromatography and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli
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
-
enhancement of the activity towards D-xylose is not observed, mutation 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
-
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
-