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show all sequences of 1.1.1.360

Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus

Angelov, A.; Fuetterer, O.; Valerius, O.; Braus, G.H.; Liebl, W.; FEBS J. 272, 1054-1062 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Picrophilus torridus
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetone
20% (v/v), 40% loss of activity
Picrophilus torridus
ATP
inhibition displays Michaelis-Menten kinetics in a noncompetitive mode with respect to the cofactor NADP+
Picrophilus torridus
ethanol
20% (v/v), 20% loss of activity
Picrophilus torridus
methanol
20% (v/v), 30% loss of activity
Picrophilus torridus
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
Picrophilus torridus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
NAD+
the precise determination of the Km for NAD+ is not possible, as it is impossible to reach saturation of the enzyme
Picrophilus torridus
1.12
-
NADP+
pH 6.5, 55°C, cosubstrate: D-glucose
Picrophilus torridus
4.5
-
D-galactose
pH 6.5, 55°C, cosubstrate: NADP+
Picrophilus torridus
10
-
D-glucose
pH 6.5, 55°C, cosubstrate: NADP+
Picrophilus torridus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
addition of 5 mM NaCl, MgCl2, MnCl2 or CaCl2 has no effect
Picrophilus torridus
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
Picrophilus torridus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40462
-
4 * 40462, calculated from sequence
Picrophilus torridus
40500
-
4 * 40500, SDS-PAGE
Picrophilus torridus
160000
-
gel filtration
Picrophilus torridus
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Acetone
50% (v/v), no detectable loss of activity
Picrophilus torridus
Ethanol
50% (v/v), no detectable loss of activity
Picrophilus torridus
Methanol
50% (v/v), no detectable loss of activity
Picrophilus torridus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Picrophilus torridus
Q6L047
-
-
Picrophilus torridus DSM 9790
Q6L047
-
-
Purification (Commentary)
Commentary
Organism
-
Picrophilus torridus
Reaction
Reaction
Commentary
Organism
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
(2)
Picrophilus torridus
D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
(1)
Picrophilus torridus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
252
-
pH 6.5, 55°C, NADP+ (cosubstrate: D-glucose)
Picrophilus torridus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus DSM 9790
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
74% of the activity with D-glucose + NADP+
668544
Picrophilus torridus
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
74% of the activity with D-glucose + NADP+
668544
Picrophilus torridus DSM 9790
D-galactonate + NADPH + 2 H+
-
-
-
?
D-glucose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus
D-gluconate + NADH + 2 H+
-
-
-
?
D-glucose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus DSM 9790
D-gluconate + NADH + 2 H+
-
-
-
?
D-glucose + NADP+ + H2O
-
668544
Picrophilus torridus
D-gluconate + NADPH + 2 H+
-
-
-
?
D-glucose + NADP+ + H2O
-
668544
Picrophilus torridus DSM 9790
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
668544
Picrophilus torridus
?
-
-
-
-
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
668544
Picrophilus torridus DSM 9790
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 40462, calculated from sequence; 4 * 40500, SDS-PAGE
Picrophilus torridus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
substrates: glucose + NADP+
Picrophilus torridus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
55
60
55°C: optimum, 60°C: 88% of maximal activity
Picrophilus torridus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
Zn2+ improves thermal stability. EDTA completely abolishes the stabilizing effect of Zn2+
Picrophilus torridus
65
-
pH 6.5, without the addition of Zn2+, t1/2: 3 h
Picrophilus torridus
70
-
pH 6.5, without the addition of Zn2+, t1/2: 5 min. At 1 mM Zn2+ the enzyme is stable for 3 h
Picrophilus torridus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Picrophilus torridus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Picrophilus torridus
NADP+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Picrophilus torridus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
5.9
-
ATP
pH 6.5, 55°C, at saturating glucose concentration (50 mM)
Picrophilus torridus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Picrophilus torridus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Picrophilus torridus
NADP+
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
Picrophilus torridus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetone
20% (v/v), 40% loss of activity
Picrophilus torridus
ATP
inhibition displays Michaelis-Menten kinetics in a noncompetitive mode with respect to the cofactor NADP+
Picrophilus torridus
ethanol
20% (v/v), 20% loss of activity
Picrophilus torridus
methanol
20% (v/v), 30% loss of activity
Picrophilus torridus
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
Picrophilus torridus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
5.9
-
ATP
pH 6.5, 55°C, at saturating glucose concentration (50 mM)
Picrophilus torridus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
NAD+
the precise determination of the Km for NAD+ is not possible, as it is impossible to reach saturation of the enzyme
Picrophilus torridus
1.12
-
NADP+
pH 6.5, 55°C, cosubstrate: D-glucose
Picrophilus torridus
4.5
-
D-galactose
pH 6.5, 55°C, cosubstrate: NADP+
Picrophilus torridus
10
-
D-glucose
pH 6.5, 55°C, cosubstrate: NADP+
Picrophilus torridus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
addition of 5 mM NaCl, MgCl2, MnCl2 or CaCl2 has no effect
Picrophilus torridus
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
Picrophilus torridus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40462
-
4 * 40462, calculated from sequence
Picrophilus torridus
40500
-
4 * 40500, SDS-PAGE
Picrophilus torridus
160000
-
gel filtration
Picrophilus torridus
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Acetone
50% (v/v), no detectable loss of activity
Picrophilus torridus
Ethanol
50% (v/v), no detectable loss of activity
Picrophilus torridus
Methanol
50% (v/v), no detectable loss of activity
Picrophilus torridus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Picrophilus torridus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
252
-
pH 6.5, 55°C, NADP+ (cosubstrate: D-glucose)
Picrophilus torridus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus DSM 9790
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
74% of the activity with D-glucose + NADP+
668544
Picrophilus torridus
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
74% of the activity with D-glucose + NADP+
668544
Picrophilus torridus DSM 9790
D-galactonate + NADPH + 2 H+
-
-
-
?
D-glucose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus
D-gluconate + NADH + 2 H+
-
-
-
?
D-glucose + NAD+ + H2O
prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+
668544
Picrophilus torridus DSM 9790
D-gluconate + NADH + 2 H+
-
-
-
?
D-glucose + NADP+ + H2O
-
668544
Picrophilus torridus
D-gluconate + NADPH + 2 H+
-
-
-
?
D-glucose + NADP+ + H2O
-
668544
Picrophilus torridus DSM 9790
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
668544
Picrophilus torridus
?
-
-
-
-
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
668544
Picrophilus torridus DSM 9790
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 40462, calculated from sequence; 4 * 40500, SDS-PAGE
Picrophilus torridus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
substrates: glucose + NADP+
Picrophilus torridus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
55
60
55°C: optimum, 60°C: 88% of maximal activity
Picrophilus torridus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
Zn2+ improves thermal stability. EDTA completely abolishes the stabilizing effect of Zn2+
Picrophilus torridus
65
-
pH 6.5, without the addition of Zn2+, t1/2: 3 h
Picrophilus torridus
70
-
pH 6.5, without the addition of Zn2+, t1/2: 5 min. At 1 mM Zn2+ the enzyme is stable for 3 h
Picrophilus torridus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Picrophilus torridus
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the Entner–Doudoroff pathway
Picrophilus torridus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the Entner–Doudoroff pathway
Picrophilus torridus
Other publictions for EC 1.1.1.360
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726594
Kanoh
Structural insight into glucos ...
Thermoplasma volcanium, Thermoplasma volcanium DSM 4299
Acta Crystallogr. Sect. D
70
1271-1280
2014
-
-
1
1
13
-
-
5
-
-
3
3
-
2
-
-
1
-
-
-
3
-
13
1
2
-
2
-
1
-
1
2
-
-
-
-
-
1
2
1
13
-
-
-
-
5
-
-
3
3
-
-
-
1
-
-
3
-
13
1
2
-
2
-
1
-
1
-
-
-
-
-
-
-
668544
Angelov
Properties of the recombinant ...
Picrophilus torridus, Picrophilus torridus DSM 9790
FEBS J.
272
1054-1062
2005
-
-
1
-
-
-
5
4
-
2
3
-
3
8
-
-
1
2
-
-
1
-
10
1
1
1
3
-
1
-
-
2
1
-
-
-
-
1
2
-
-
-
-
5
1
4
-
2
3
-
3
-
-
1
-
-
1
-
10
1
1
1
3
-
1
-
-
-
-
1
1
-
-
-