Literature summary for 1.1.1.360 extracted from

Angelov, A.; Fuetterer, O.; Valerius, O.; Braus, G.H.; Liebl, W.
Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus (2005), FEBS J., 272, 1054-1062.

Search for more literature for 1.1.1.360

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Picrophilus torridus

Inhibitors

Inhibitors	Comment	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	Comment	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	Comment	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]	Comment	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	Comment	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	UniProt	Comment	Textmining
Picrophilus torridus	Q6L047	-	-
Picrophilus torridus DSM 9790	Q6L047	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Picrophilus torridus

Reaction

Reaction	Comment	Organism	Reaction ID
D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+	(2)	Picrophilus torridus	a
D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+	(1)	Picrophilus torridus	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
252	-	pH 6.5, 55°C, NADP+ (cosubstrate: D-glucose)	Picrophilus torridus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-galactose + NAD+ + H2O	prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+	Picrophilus torridus	D-galactonate + NADH + 2 H+	-	?
D-galactose + NAD+ + H2O	prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+	Picrophilus torridus DSM 9790	D-galactonate + NADH + 2 H+	-	?
D-galactose + NADP+ + H2O	74% of the activity with D-glucose + NADP+	Picrophilus torridus	D-galactonate + NADPH + 2 H+	-	?
D-galactose + NADP+ + H2O	74% of the activity with D-glucose + NADP+	Picrophilus torridus DSM 9790	D-galactonate + NADPH + 2 H+	-	?
D-glucose + NAD+ + H2O	prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+	Picrophilus torridus	D-gluconate + NADH + 2 H+	-	?
D-glucose + NAD+ + H2O	prefers NADP+ over NAD+. Approximately 20-fold higher activity with NADP+	Picrophilus torridus DSM 9790	D-gluconate + NADH + 2 H+	-	?
D-glucose + NADP+ + H2O	-	Picrophilus torridus	D-gluconate + NADPH + 2 H+	-	?
D-glucose + NADP+ + H2O	-	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	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	Picrophilus torridus DSM 9790	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 40462, calculated from sequence	Picrophilus torridus
tetramer	4 * 40500, SDS-PAGE	Picrophilus torridus

Synonyms

Synonyms	Comment	Organism
dual-specific glucose/galactose dehydrogenase	-	Picrophilus torridus
GdhA	-	Picrophilus torridus
glucose (galactose) dehydrogenase	-	Picrophilus torridus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
55	-	substrates: glucose + NADP+	Picrophilus torridus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	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]	Comment	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	Comment	Organism
6.5	-	-	Picrophilus torridus

Cofactor

Cofactor	Comment	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	Comment	Organism	Structure
5.9	-	ATP	pH 6.5, 55°C, at saturating glucose concentration (50 mM)	Picrophilus torridus

General Information

General Information	Comment	Organism
physiological function	the enzyme is involved in glucose catabolism via a nonphosphorylated variant of the EntnerDoudoroff pathway	Picrophilus torridus

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Release 2023.1 (January 2023)