Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
Substrates: -
Products: -
?
(R)-indanol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
(R)-tetralol + NAD+
3,4-dihydronaphthalen-2(1H)-one + NADH + H+
Substrates: -
Products: -
?
(R)-tetralol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
(S)-(+)-1,2,3,4-tetrahydro-1-naphthol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
(S)-(+)-1-indanol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
(S)-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
Substrates: -
Products: -
?
(S)-indanol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
(S)-tetralol + NAD+
3,4-dihydronaphthalen-2(1H)-one + NADH + H+
Substrates: -
Products: -
?
(S)-tetralol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
1-acenaphthenol + NAD+
? + NADH + H+
2,3,4-trideoxyaldopyranose + NAD+
? + NADH
-
Substrates: -
Products: -
?
2-cyclohexen-1-ol + NAD+
2-cyclohexen-1-one + NADH + H+
Substrates: -
Products: -
?
2-cyclohexen-1-ol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
2-deoxy-D-galactose + NAD+
2-deoxy-D-galactono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
2-deoxy-D-galactose + NAD+
? + NADH
-
Substrates: -
Products: -
?
2-deoxy-D-galactose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Substrates: relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
2-deoxy-D-glucose + NAD+
? + NADH
-
Substrates: -
Products: -
?
2-deoxy-D-glucose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
Substrates: relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
Products: -
?
4-chromanol + NAD+
2,3-dihydro-4H-chromen-4-one + NADH + H+
Substrates: -
Products: -
?
4-chromanol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
5-hydroxypentanal + NAD+
? + NADH
-
Substrates: -
Products: -
?
6-deoxy-D-glucose
? + NADH + H+
Substrates: -
Products: -
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
alpha-tetralone + NADH + H+
? + NAD+
Substrates: -
Products: -
?
cellobiose + NAD+
? + NADH + H+
chalcose + NAD+
? + NADH
-
Substrates: demethylated
Products: -
?
cis-benzene dihydrodiol + NAD+
? + NADH + H+
D-aldose + NAD+
D-aldonolactone + NADH
D-allose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-altrose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
D-fucose + NAD+
D-fucono-delta-lactone + NADH + H+
D-galactosamine + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-galactosamine + NAD+
D-galactosamino-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
D-galactose + NAD+
D-galactono-gamma-lactone + NADH + H+
Substrates: -
Products: -
?
D-glucosamine + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-glucosamine + NAD+
D-glucosamino-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: activity is 23% compared to the activity with D-mannose and NAD+. No activity with beta-D-glucose + NADP+
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
D-mannose + NAD+
? + NADH
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
Substrates: relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
Substrates: relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+
Products: -
?
D-quinovose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-talose + NAD+
? + NADH + H+
D-xylose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Substrates: relative activity with D-xylose and NADP+ is less than 5% compared to the activity with D-xylose and NAD+
Products: -
?
D-xylose + NAD+
D-xylono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: relative activity with D-xylose and NADP+ is less than 5% compared to the activity with D-xylose and NAD+
Products: -
?
glucono-delta-lactone + NADH + H+
? + NAD+
Substrates: -
Products: -
?
isatin + NADH + H+
? + NAD+
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH
L-arabinose + NAD+
? + NADH + H+
L-fucose + NAD+
? + NADH + H+
lactose + NAD+
? + NADH + H+
phenyl-1,2-propanedione + NADH + H+
? + NAD+
Substrates: -
Products: -
?
viosamine + NAD+
? + NADH
-
Substrates: i.e. 4-amino-4,6-dideoxy-D-glucose
Products: -
?
additional information
?
-
1-acenaphthenol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
1-acenaphthenol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
cellobiose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
cellobiose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
cis-benzene dihydrodiol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
cis-benzene dihydrodiol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: broad substrate specificity
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: -
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: broad substrate specificity
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: the enzyme is coordinately regulated with EC 1.1.1.120 and EC 1.1.1.117
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: D-aldoses of pyranose ring size
Products: -
?
D-aldose + NAD+
D-aldonolactone + NADH
-
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
-
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
-
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
-
Substrates: -
Products: hydrolyzes spontaneously to D-fuconate
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
-
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-fucose + NAD+
D-fucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
Substrates: beta-anomer preferred to alpha-anomer
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
Substrates: -
Products: -
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: the most probable produced aldonolactones from this and the following substrates have not been isolated so far
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: the most probable produced aldonolactones from this and the following substrates have not been isolated so far
Products: -
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: beta-anomer preferred over alpha-anomer
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: beta-anomer preferred over alpha-anomer
Products: -
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: the most probable produced aldonolactones from this and the following substrates have not been isolated so far
Products: -
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
Substrates: -
Products: -
?
D-mannose + NAD+
?
-
Substrates: -
Products: -
r
D-mannose + NAD+
?
-
Substrates: AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-mannose, the enzyme catalyzes the oxidation of several monosaccharides with a preference for NAD+ rather than NADP+ as a cofactor. Conformation of the Glu side-chain is crucial for discrimination between D-mannose and its C2 epimer D-glucose, and the conformation of the glutamate side-chain depends on the spatial arrangement of nearby hydrophobic residues that do not directly interact with the substrate, D-mannose recognition mechanism of AldT and inter-subunit interactions, overview
Products: -
r
D-mannose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-mannose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-talose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-talose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-xylose + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-xylose + NAD+
? + NADH
-
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH
-
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH
-
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH
-
Substrates: alpha-anomer preferred to beta-anomer
Products: -
?
L-arabinose + NAD+
? + NADH
-
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
L-arabinose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
L-fucose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
L-fucose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
lactose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
lactose + NAD+
? + NADH + H+
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: substrates are D-aldoses of pyranose ring size
Products: -
?
additional information
?
-
-
Substrates: L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
Products: -
?
additional information
?
-
-
Substrates: NADP+ ineffective as cofactor at concentrations up to 20 mM
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: substrates are D-aldoses of pyranose ring size
Products: -
?
additional information
?
-
-
Substrates: L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
Products: -
?
additional information
?
-
-
Substrates: NADP+ ineffective as cofactor at concentrations up to 20 mM
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
?
additional information
?
-
-
Substrates: structural insights into substrate selectivity of AldT, overview
Products: -
?
additional information
?
-
Substrates: TAD possesses the catalytic triad Ser136, Tyr149, and Lys153. No activity with L-xylose, D-ribose and 2-deoxy-D-ribose. TAD does not oxidize ketoses (D-fructose and D-sorbose), sugar alcohols (D-sorbitol, galactitol, inositol, L-arabitol and xylitol), uronic acids (D-galacturonic acid and D-glucuronic acid), aldonic acids (L-gulonic acid and 2-keto-L-gulonic acid), aromatic alcohols (benzyl alcohol and catechol), aliphatic alcohols (1-nonanol, 1-decanol, 3-hydroxybutyric acid and 2,3-butanediol), and hydroxysteroids (androsterone, testosterone, 20alpha/beta-hydroxyprogesterone, cholic acid, cortisol and corticosterone). No significant activity ketones (4-nitroacetophenone, camphorquinone, 2,3-hexanedione and diacetyl) and aldehydes (4-nitrobenzaldehyde, pyridine-3-aldehyde, 1-nonanal and citral)
Products: -
?
additional information
?
-
-
Substrates: TAD possesses the catalytic triad Ser136, Tyr149, and Lys153. No activity with L-xylose, D-ribose and 2-deoxy-D-ribose. TAD does not oxidize ketoses (D-fructose and D-sorbose), sugar alcohols (D-sorbitol, galactitol, inositol, L-arabitol and xylitol), uronic acids (D-galacturonic acid and D-glucuronic acid), aldonic acids (L-gulonic acid and 2-keto-L-gulonic acid), aromatic alcohols (benzyl alcohol and catechol), aliphatic alcohols (1-nonanol, 1-decanol, 3-hydroxybutyric acid and 2,3-butanediol), and hydroxysteroids (androsterone, testosterone, 20alpha/beta-hydroxyprogesterone, cholic acid, cortisol and corticosterone). No significant activity ketones (4-nitroacetophenone, camphorquinone, 2,3-hexanedione and diacetyl) and aldehydes (4-nitrobenzaldehyde, pyridine-3-aldehyde, 1-nonanal and citral)
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Green, P.N.; Gibson, D.M.
Carbohydrate metabolism in some methylotrophic bacteria
FEMS Microbiol. Lett.
23
31-34
1984
Methylobacterium mesophilicum, Methylobacterium organophilum, Methylobacterium organophilum XX, Pseudomonas sp., Pseudomonas sp. NCIB10602 NCIB10603
-
brenda
Cline, A.L.; Hu, A.S.L.
The isolation of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4488-4492
1965
Pseudomonas sp., Pseudomonas sp. G6
brenda
Cline, A.L.; Hu, A.S.L.
Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4493-4497
1965
Pseudomonas sp., Pseudomonas sp. G6
brenda
Dahms, A.S.; Anderson, R.L.
D-Fucose metabolism in a pseudomonad. I. Oxidation of D-fucose to D-fucono-delta-lactone by a D-aldohexose dehydrogenase
J. Biol. Chem.
247
2222-2227
1972
Pseudomonas sp., Pseudomonas sp. MSU-1
brenda
Cline, A.L.; Hu, A.S.L.
Some physical properties of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4498-4502
1965
Pseudomonas sp., Pseudomonas sp. G6
brenda
Yasutake, Y.; Nishiya, Y.; Tamura, N.; Tamura, T.
Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase
J. Mol. Biol.
367
1034-1046
2007
Thermoplasma acidophilum
brenda
Asada, Y.; Endo, S.; Inoue, Y.; Mamiya, H.; Hara, A.; Kunishima, N.; Matsunaga, T.
Biochemical and structural characterization of a short-chain dehydrogenase/reductase of Thermus thermophilus HB8: a hyperthermostable aldose-1-dehydrogenase with broad substrate specificity
Chem. Biol. Interact.
178
117-126
2009
Thermus thermophilus HB8 (Q5SLC4), Thermus thermophilus HB8
brenda
Yasutake, Y.; Nishiya, Y.; Tamura, N.; Tamura, T.
Crystallization and preliminary crystallographic analysis of NAD+-preferring aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum
Acta Crystallogr. Sect. F
62
586-589
2006
Thermoplasma acidophilum (Q9HK51), Thermoplasma acidophilum
brenda
Nishiya, Y.; Tamura, N.; Tamura, T.
Analysis of bacterial glucose dehydrogenase homologs from thermoacidophilic archaeon Thermoplasma acidophilum: finding and characterization of aldohexose dehydrogenase
Biosci. Biotechnol. Biochem.
68
2451-2456
2004
Thermoplasma acidophilum (Q9HK51), Thermoplasma acidophilum
brenda
Asada, Y.; Endo, S.; Inoue, Y.; Mamiya, H.; Hara, A.; Kunishima, N.; Matsunaga, T.
Biochemical and structural characterization of a short-chain dehydrogenase/reductase of Thermus thermophilus HB8. A hyperthermostable aldose-1-dehydrogenase with broad substrate specificity
Chem. Biol. Interact.
178
117-126
2009
Thermus thermophilus (Q5SLC4)
brenda