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Information on EC 1.1.1.121 - aldose 1-dehydrogenase (NAD+)
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1.1.1.121 aldose 1-dehydrogenase (NAD+)IUBMB Comments
Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
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Word Map
- 1.1.1.121
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electrode
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biosensors
- gluconobacter
-
osmium
- ferrocene
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cathode
- nadp+
- acidophilum
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pqq-dependent
- thermophilus
- archaeon
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voltage
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mass-producible
- oxydans
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thermoplasma
- d-fucose
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thermoacidophilic
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electrochemical
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anode
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biofuel
-
printed
- xylose
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benchmark
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graphite
- laccase
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aldose dehydrogenase, ta0754, aldohexose dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldose dehydrogenase
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dehydrogenase, D-aldohexose
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additional information
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the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-aldose + NAD+ = D-aldonolactone + NADH + H+
acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and xylose
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-
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D-aldose + NAD+ = D-aldonolactone + NADH + H+
catalytic mechanism involving a conserved catalytic triad Ser-Tyr-Lys at the catalytic site, the C-terminal tail shuts the substrate-binding pocket, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
D-aldose:NAD+ 1-oxidoreductase
Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
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CAS REGISTRY NUMBER
COMMENTARY
9076-61-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
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-
-
?
(R)-tetralol + NAD+
3,4-dihydronaphthalen-2(1H)-one + NADH + H+
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-
?
(S)-(+)-1,2,3,4-tetrahydro-1-naphthol + NAD+
? + NADH + H+
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-
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?
(S)-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
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-
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?
(S)-tetralol + NAD+
3,4-dihydronaphthalen-2(1H)-one + NADH + H+
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-
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?
2-deoxy-D-galactose + NAD+
2-deoxy-D-galactono-delta-lactone + NADH + H+
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?
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+
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-delta-lactone + NADH + H+
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?
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+
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?
4-chromanol + NAD+
2,3-dihydro-4H-chromen-4-one + NADH + H+
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?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-delta-lactone + NADH + H+
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?
D-galactosamine + NAD+
D-galactosamino-delta-lactone + NADH + H+
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?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH + H+
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-
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?
D-glucosamine + NAD+
D-glucosamino-delta-lactone + NADH + H+
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-
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?
D-glucose + NAD+
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+
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?
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+
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?
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+
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?
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+
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?
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+
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?
D-aldose + NAD+
D-aldonolactone + NADH
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broad substrate specificity
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?
D-aldose + NAD+
D-aldonolactone + NADH
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broad substrate specificity
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?
D-aldose + NAD+
D-aldonolactone + NADH
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the enzyme is coordinately regulated with EC 1.1.1.120 and EC 1.1.1.117
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?
D-aldose + NAD+
D-aldonolactone + NADH
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D-aldoses of pyranose ring size
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?
D-fucose + NAD+
D-fucono-delta-lactone + NADH
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hydrolyzes spontaneously to D-fuconate
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
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beta-anomer preferred to alpha-anomer
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?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
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?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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the most probable produced aldonolactones from this and the following substrates have not been isolated so far
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?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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the most probable produced aldonolactones from this and the following substrates have not been isolated so far
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r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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beta-anomer preferred over alpha-anomer
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?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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beta-anomer preferred over alpha-anomer
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r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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the most probable produced aldonolactones from this and the following substrates have not been isolated so far
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r
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
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?
D-mannose + NAD+
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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
?
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substrates are D-aldoses of pyranose ring size
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?
additional information
?
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L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
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?
additional information
?
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NADP+ ineffective as cofactor at concentrations up to 20 mM
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?
additional information
?
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substrates are D-aldoses of pyranose ring size
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?
additional information
?
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L-aldohexoses, ketohexoses, pentoses, trioses, polyols, di- and trisaccharides, derivatives of D-aldohexoses are no substrates
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?
additional information
?
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NADP+ ineffective as cofactor at concentrations up to 20 mM
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?
additional information
?
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broad substrate specificity
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?
additional information
?
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structural insights into substrate selectivity of AldT, overview
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additional information
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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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?
additional information
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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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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-aldose + NAD+
D-aldonolactone + NADH
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broad substrate specificity
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?
D-aldose + NAD+
D-aldonolactone + NADH
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broad substrate specificity
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?
D-aldose + NAD+
D-aldonolactone + NADH
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the enzyme is coordinately regulated with EC 1.1.1.120 and EC 1.1.1.117
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?
D-aldose + NAD+
D-aldonolactone + NADH
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D-aldoses of pyranose ring size
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
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preference for NAD+ rather than NADP+ as a cofactor, binding site structure, overview
NAD+
relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+. Relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
NADP+
relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+. Relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
additional information
TAD does not exhibit dehydrogenase activity with NADP+ as the coenzyme
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additional information
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TAD does not exhibit dehydrogenase activity with NADP+ as the coenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
2,3-benzofuran
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
Hexestrol
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
indole
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
additional information
EDTA (1 mM) and p-chloromercuriphenylsulfonate and p-chloromercuribenzoate (0.1 mM) have no effect on the activity
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additional information
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EDTA (1 mM) and p-chloromercuriphenylsulfonate and p-chloromercuribenzoate (0.1 mM) have no effect on the activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
kcat and Km values are increased by the elevation of temperature, whereas the kcat/Km values are not largely changed
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additional information
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kcat and Km values are increased by the elevation of temperature, whereas the kcat/Km values are not largely changed
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE