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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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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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+)).
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
with NADP+ (2 mM) as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose (100 mM substrate), and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
with NADP+ as the electron acceptor, the enzyme acts exclusively on D-glucose and D-galactose, and the activity towards D-galactose is 58% of that observed towards D-glucose. The activities with D-xylose, L-arabinose, D-ribose, D-fructose and D-mannose are all less than 4% of that with D-glucose
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
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
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
the enzyme utilizes NAD+ as a cofactor with nearly the same substrate specificity as NADP, but the electron-acceptor activity of NAD+ (2 mM) is only 4% of that observed with NADP+ (at 100 mM D-glucose)
the enzyme utilizes NAD+ as a cofactor with nearly the same substrate specificity as NADP, but the electron-acceptor activity of NAD+ (2 mM) is only 4% of that observed with NADP+ (at 100 mM D-glucose)
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
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
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
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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
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
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
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