Information on EC 1.1.1.121 - aldose 1-dehydrogenase (NAD+)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.121
-
RECOMMENDED NAME
GeneOntology No.
aldose 1-dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-aldose + NAD+ = D-aldonolactone + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-61-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain XX
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-
Manually annotated by BRENDA team
strain XX
-
-
Manually annotated by BRENDA team
MSU-1
-
-
Manually annotated by BRENDA team
NCIB10602, NCIB10603
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-indanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
(R)-tetralol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
(S)-(+)-1,2,3,4-tetrahydro-1-naphthol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
(S)-(+)-1-indanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
(S)-indanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
(S)-tetralol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
1-acenaphthenol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
2,3,4-trideoxyaldopyranose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
2-cyclohexen-1-ol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
2-deoxy-D-galactose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
2-deoxy-D-galactose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
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 + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
2-deoxy-D-glucose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
relative activity with 2-deoxy-D-glucose and NADP+ is less than 5% compared to the activity with 2-deoxy-D-glucose and NAD+
-
-
?
4-chromanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
5-hydroxypentanal + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
6-deoxy-D-glucose
? + NADH + H+
show the reaction diagram
-
-
-
?
alpha-tetralone + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
cellobiose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
chalcose + NAD+
? + NADH
show the reaction diagram
-
demethylated
-
-
-
cis-benzene dihydrodiol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-aldose + NAD+
D-aldonolactone + NADH
show the reaction diagram
D-allose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
D-altrose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
D-fucose + NAD+
D-fucono-delta-lactone + NADH
show the reaction diagram
D-fucose + NAD+
D-fucono-delta-lactone + NADH + H+
show the reaction diagram
-
-
-
?
D-galactosamine + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-galactose + NAD+
D-galactono-gamma-lactone + NADH
show the reaction diagram
D-galactose + NAD+
D-galactono-gamma-lactone + NADH + H+
show the reaction diagram
-
-
-
?
D-glucosamine + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
activity is 23% compared to the activity with D-mannose and NAD+. No activity with beta-D-glucose + NADP+
-
-
?
D-glucose + NAD+
D-glucono-delta-lactone + NADH + H+
show the reaction diagram
D-mannose + NAD+
?
show the reaction diagram
D-mannose + NAD+
? + NADH
show the reaction diagram
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
show the reaction diagram
-
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
show the reaction diagram
-
relative activity with D-mannose and NADP+ is 7% compared to the activity with D-mannose and NAD+
-
-
?
D-quinovose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
-
D-talose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-xylose + NAD+
? + NADH
show the reaction diagram
D-xylose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
-
relative activity with D-xylose and NADP+ is less than 5% compared to the activity with D-xylose and NAD+
-
-
?
glucono-delta-lactone + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
isatin + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
L-arabinose + NAD+
? + NADH
show the reaction diagram
L-arabinose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
L-fucose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
lactose + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
phenyl-1,2-propanedione + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
viosamine + NAD+
? + NADH
show the reaction diagram
-
i.e. 4-amino-4,6-dideoxy-D-glucose
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-aldose + NAD+
D-aldonolactone + NADH
show the reaction diagram
D-mannose + NAD+
?
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
TAD does not exhibit dehydrogenase activity with NADP+ as the coenzyme
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
kcat and Km values are increased by the elevation of temperature, whereas the kcat/Km values are not largely changed
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
(S)-tetralol
-
0.14
1-Acenaphthenol
-
3.7
2-Cyclohexen-1-ol
-
6.3 - 33
2-deoxy-D-galactose
1.6 - 300
2-deoxy-D-glucose
178
6-deoxy-D-glucose
-
1.9
alpha-tetralone
-
27
cis-benzene dihydrodiol
-
13
D-Allose
-
-
2.4
D-Altrose
-
-
5.5 - 5.8
D-fucose
2 - 3
D-galactosamine
-
0.78 - 78
D-galactose
139
D-glucosamine
-
0.86 - 580
D-glucose
4.5 - 25
D-mannose
0.08 - 0.25
NAD+
2
phenyl-1,2-propanedione
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.167
(R)-indanol
Thermus thermophilus HB8
Q5SLC4
-
0.075
(R)-tetralol
Thermus thermophilus HB8
Q5SLC4
-
138.7
(S)-indanol
Thermus thermophilus HB8
Q5SLC4
-
161.7
(S)-tetralol
Thermus thermophilus HB8
Q5SLC4
-
433.3
1-Acenaphthenol
Thermus thermophilus HB8
Q5SLC4
-
3.5
2-Cyclohexen-1-ol
Thermus thermophilus HB8
Q5SLC4
-
12.8
2-deoxy-D-galactose
Thermus thermophilus HB8
Q5SLC4
-
6.93
2-deoxy-D-glucose
Thermus thermophilus HB8
Q5SLC4
-
40.3
4-chromanol
Thermus thermophilus HB8
Q5SLC4
-
6.35
6-deoxy-D-glucose
Thermus thermophilus HB8
Q5SLC4
-
3.9
alpha-tetralone
Thermus thermophilus HB8
Q5SLC4
-
5.767
cellobiose
Thermus thermophilus HB8
Q5SLC4
-
7.383
cis-benzene dihydrodiol
Thermus thermophilus HB8
Q5SLC4
-
8.73
D-fucose
Thermus thermophilus HB8
Q5SLC4
-
0.3117
D-galactosamine
Thermus thermophilus HB8
Q5SLC4
-
8.25
D-galactose
Thermus thermophilus HB8
Q5SLC4
-
0.6217
D-glucosamine
Thermus thermophilus HB8
Q5SLC4
-
3.85
D-glucose
Thermus thermophilus HB8
Q5SLC4
-
3.017
D-talose
Thermus thermophilus HB8
Q5SLC4
-
0.423
D-xylose
Thermus thermophilus HB8
Q5SLC4
-
981.7
isatin
Thermus thermophilus HB8
Q5SLC4
-
4.55
L-arabinose
Thermus thermophilus HB8
Q5SLC4
-
0.1067
L-fucose
Thermus thermophilus HB8
Q5SLC4
-
9.23
lactose
Thermus thermophilus HB8
Q5SLC4
-
16.83
phenyl-1,2-propanedione
Thermus thermophilus HB8
Q5SLC4
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
1,10-phenanthroline
-
0.042
2,3-benzofuran
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
1,10-phenanthroline
Thermus thermophilus HB8
Q5SLC4
-
0.2
2,3-benzofuran
Thermus thermophilus HB8
Q5SLC4
-
1.2
catechol
Thermus thermophilus HB8
Q5SLC4
-
0.063
Hexestrol
Thermus thermophilus HB8
Q5SLC4
-
1.9
indazole
Thermus thermophilus HB8
Q5SLC4
-
0.48
indole
Thermus thermophilus HB8
Q5SLC4
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
pH 8.0, 37C, substrates: D-glucose + NAD+
15
-
pH 8.0, 37C, substrates: D-xylose + NAD+
24
-
pH 8.0, 37C, substrates: 2-deoxy-D-glucose + NAD+
31
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pH 8.0, 37C, substrates: D-mannose + NAD+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
Tris/HCl buffer
9 - 10
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glycine/NaOH buffer
9.2
-
Tris/acetate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.3
-
66% of maximal activity at pH 7.2 and pH 9.3 in Tris/HCl buffer
8 - 9.8
-
about 80% of maximal activity at pH 8.0 and 9.8 in Tris/acetate buffer
8.5 - 10.4
-
about 80% of maximal activity at pH 8.5 and 10.4 in glycine/NaOH buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
25
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
gel filtration
85000
-
gel filtration
100000
gel filtration
140000
-
sedimentation analysis in EDTA/phosphate buffer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 27000, SDS-PAGE
additional information
-
the AldT subunit forms a typical SDR fold with an unexpectedly long C-terminal tail and assembles into an intertwined tetramer, inter-subunit interactions, crystal structure, structure comparison, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique at 20C under several acidic conditions with polyethylene glycol and ammonium sulfate as precipitants. Optimization of the initial crystallizations conditions yields single crystals in solution containing 0.1 M sodium acetate pH 4.6, 18%(w/v) PEG 4000, 0.2 M ammonium sulfate and 15%(v/v) glycerol. An X-ray diffraction data set is collected to a resolution of 2.8 A
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purified recombinant AldT in ligand-free form, in complex with NADH, and in complex with the substrate D-mannose, hanging drop or sitting drop vapor diffusion method, 20C, 8 mg/ml protein and 4 mM mM beta-NADH, mixing of 0.001-0.0025 ml of reservoir solution and sample solution, and equilibration against 0.5 ml of reservoir solution, streak-seeding method, from 0.1 M sodium acetate, pH 5.0, 0.2 M ammonium sulfate, 16% w/v PEG 3350, and 15% v/v glycerol, or from 0.1 M sodium acetate, pH 5.0-5.4, 0.2 M ammonium sulfate, 14-18% PEG 3350, and 15-20% glycerol, X-ray diffraction structure determination and analysis at 2.1 A, 1.65 A, and 1.6 A resolution, respectively, modelling
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by oil-microbatch method, at 1.65 A resolution. TAD follows an ordered sequential mechanism in which the coenzyme binds first
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
25C, 16 h, no loss of activity
719111
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
-
half-life: 1 min, biphasic inactivation curve
50
-
rapidly inactivated
55
-
half-life: 40 s in sodium phosphate buffer, pH 7.0, with D-fucose, D-galactose, D-glucose or D-mannose as substrate
60
-
stable up to, pH 7.5, 15 min
85
approximately 40% of the activity is inactivated by the incubation of the enzyme solution (0.3 mg/ml in 10 mM potassium phosphate, pH 7.0) for 15 min at 95C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, acetone-dried cells retain full activity over a long period
-
-20C, Sephadex G-200 fractions are stable for at least 6 months
-
5C, in presence of 2-mercaptoethanol 50% loss of activity after several months
-
frozen, stable for many months
-
lyophilized, stable for many months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by sonication, heating at 70C for 10 min, ion-exchange chromatography, gel filtration and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aldT, overexpression of His-tagged enzyme in Escherichia coli strain BL21
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into vector pET-11a and overexpressed in Escherichia coli BL21 (DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D242N
mutation results in a large decrease in thermostability of TAD without dissociation into dimer or monomer
F141A
mutation results in decrease in thermostability of TAD without dissociation into dimer or monomer
F249A
mutation results in decrease in thermostability of TAD without dissociation into dimer or monomer