1.1.1.121: aldose 1-dehydrogenase (NAD+)
This is an abbreviated version, for detailed information about aldose 1-dehydrogenase (NAD+), go to the full flat file.
Reaction
Synonyms
aldohexose dehydrogenase, aldose dehydrogenase, AldT, D-aldohexose dehydrogenase, dehydrogenase, D-aldohexose, More, Ta0754, TAD
ECTree
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10
22
Substrates Products
Substrates Products on EC 1.1.1.121 - aldose 1-dehydrogenase (NAD+)
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REACTION DIAGRAM
(S)-(+)-1,2,3,4-tetrahydro-1-naphthol + NAD+
? + NADH + H+
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
-
-
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
activity is 23% compared to the activity with D-mannose and NAD+. No activity with beta-D-glucose + NADP+
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
relative activity with D-xylose and NADP+ is less than 5% compared to the activity with D-xylose and NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
relative activity with D-xylose and NADP+ is less than 5% compared to the activity with D-xylose and NAD+
-
-
?
D-aldonolactone + NADH
-
broad substrate specificity
-
-
-
D-aldose + NAD+
D-aldonolactone + NADH
-
broad substrate specificity
-
-
-
D-aldose + NAD+
D-aldonolactone + NADH
-
the enzyme is coordinately regulated with EC 1.1.1.120 and EC 1.1.1.117
-
-
-
D-aldose + NAD+
D-aldonolactone + NADH
-
D-aldoses of pyranose ring size
-
-
-
D-fucose + NAD+
D-fucono-delta-lactone + NADH
-
-
hydrolyzes spontaneously to D-fuconate
-
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
beta-anomer preferred to alpha-anomer
-
-
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
-
-
-
-
D-glucono-delta-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
the most probable produced aldonolactones from this and the following substrates have not been isolated so far
-
-
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
the most probable produced aldonolactones from this and the following substrates have not been isolated so far
-
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
beta-anomer preferred over alpha-anomer
-
-
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
beta-anomer preferred over alpha-anomer
-
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
the most probable produced aldonolactones from this and the following substrates have not been isolated so far
-
r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
-
-
-
-
D-mannose + NAD+
?
-
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
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-
r
additional information
?
-
-
substrates are D-aldoses of pyranose ring size
-
-
-
additional information
?
-
-
L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
-
-
-
additional information
?
-
-
NADP+ ineffective as cofactor at concentrations up to 20 mM
-
-
-
additional information
?
-
-
substrates are D-aldoses of pyranose ring size
-
-
-
additional information
?
-
-
L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
-
-
-
additional information
?
-
-
NADP+ ineffective as cofactor at concentrations up to 20 mM
-
-
-
additional information
?
-
-
broad substrate specificity
-
-
-
additional information
?
-
-
structural insights into substrate selectivity of AldT, overview
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-
-
additional information
?
-
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)
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