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Information on EC 1.1.1.360 - glucose/galactose 1-dehydrogenase and Organism(s) Picrophilus torridus and UniProt Accession Q6L047

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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+)).
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Picrophilus torridus
UNIPROT: Q6L047
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The taxonomic range for the selected organisms is: Picrophilus torridus
The enzyme appears in selected viruses and cellular organisms
Synonyms
dual-specific glucose/galactose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dual-specific glucose/galactose dehydrogenase
-
glucose (galactose) dehydrogenase
-
glucose/galactose dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
(1)
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
show the reaction diagram
(2)
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+)).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
show the reaction diagram
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
show the reaction diagram
74% of the activity with D-glucose + NADP+
-
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
show the reaction diagram
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
-
-
?
D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
NADP+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with 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
INHIBITOR
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
4.5
D-galactose
pH 6.5, 55°C, cosubstrate: NADP+
10
D-glucose
pH 6.5, 55°C, cosubstrate: NADP+
1.12
NADP+
pH 6.5, 55°C, cosubstrate: D-glucose
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
252
pH 6.5, 55°C, NADP+ (cosubstrate: D-glucose)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
substrates: glucose + NADP+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
55°C: optimum, 60°C: 88% of maximal activity
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
gel filtration
40462
4 * 40462, calculated from sequence
40500
4 * 40500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
50% (v/v), no detectable loss of activity
Ethanol
50% (v/v), no detectable loss of activity
Methanol
50% (v/v), no detectable loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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)
Manually annotated by BRENDA team