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EC Tree
IUBMB Comments Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
The taxonomic range for the selected organisms is: Arabidopsis thaliana The enzyme appears in selected viruses and cellular organisms
Synonyms
aldh2, aldh1, aldh1a1, aldehyde dehydrogenase 2, aldh1a3, aldh3a1, aldehyde dehydrogenase 1, aldh1a2, mitochondrial aldehyde dehydrogenase, aldehyde dehydrogenase-2,
more
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Aldehyde dehydrogenase [NAD+]
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Aldehyde dehydrogenase, cytosolic
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Aldehyde dehydrogenase, microsomal
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aldehyde:NAD+ oxidoreductase
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Allergen Alt a 10
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Brassica turgor-responsive/drought-induced gene 26 protein
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CoA-independent aldehyde dehydrogenase
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gamma-aminobutyraldehyde dehydrogenase
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K(+)-activated acetaldehyde dehydrogenase
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m-methylbenzaldehyde dehydrogenase
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Matured fruit 60 kDa protein
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Mg(2+)-activated acetaldehyde dehydrogenase
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NAD+-linked aldehyde dehydrogenase
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NAD-aldehyde dehydrogenase
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NAD-dependent 4-hydroxynonenal dehydrogenase
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NAD-dependent aldehyde dehydrogenase
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NAD-linked aldehyde dehydrogenase
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propionaldehyde dehydrogenase
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R-aminobutyraldehyde dehydrogenase
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Retinal dehydrogenase
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Turgor-responsive protein 26G
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ALDH3H1
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cytosolic isoform
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KEGG
Arginine and proline metabolism , Ascorbate and aldarate metabolism , beta-Alanine metabolism , Biosynthesis of secondary metabolites , Chloroalkane and chloroalkene degradation , Fatty acid degradation , Glycerolipid metabolism , Glycolysis / Gluconeogenesis , Histidine metabolism , Insect hormone biosynthesis , Limonene and pinene degradation , Lysine degradation , Microbial metabolism in diverse environments , Pantothenate and CoA biosynthesis , Pyruvate metabolism , Tryptophan metabolism , Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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aldehyde:NAD+ oxidoreductase
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
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(E)-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
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?
4-hydroxynonenal + NAD+ + H2O
? + NADH + H+
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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-
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-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
hexanal + NAD+ + H2O
hexanoate + NADH + H+
nonanal + NAD+ + H2O
nonanoate + NADH + H+
octanal + NAD+ + H2O
octanoate + NADH + H+
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?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
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-
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?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
trans-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
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?
additional information
?
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dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
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?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
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best substrate
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?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
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?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
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?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
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?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
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?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
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?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
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?
additional information
?
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no activity with NADP+
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?
additional information
?
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no activity with NADP+
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?
additional information
?
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no activity with NADP+. Saturated aldehydes are preferred over unsaturated aldehydes, irrespective of chain length
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?
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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?
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NAD+
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NAD+
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dependent on, no activity with NADP+
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0.0403
4-hydroxynonenal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.005
dodecanal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.029
octanal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.51
propionaldehyde
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.18 - 0.199
trans-2-hexenal
0.003 - 0.0322
trans-2-nonenal
0.071
hexanal
wild type enzyme, at pH 8.0 and 25°C
0.071
hexanal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.072
hexanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.119
NAD+
-
wild type enzyme, with nonanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.421
NAD+
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wild type enzyme, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.421
NAD+
wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.441
NAD+
mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.496
NAD+
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mutant enzyme I200V, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.496
NAD+
mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.564
NAD+
mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
0.63
NAD+
mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.886
NAD+
mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.991
NAD+
mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.992
NAD+
mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.068
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
1.092
NAD+
mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
1.262
NAD+
mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.622
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
1.648
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.649
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
1.829
NAD+
mutant enzyme E149T/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
1.856
NAD+
mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
2.115
NAD+
mutant enzyme E149T/V178R/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
2.524
NAD+
mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.218
NAD+
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mutant enzyme I200G, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C
3.218
NAD+
mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.418
NAD+
mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
3.651
NAD+
mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
4.059
NAD+
mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
4.136
NAD+
mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
0.008
Nonanal
wild type enzyme, at pH 8.0 and 25°C
0.008
Nonanal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.065
Nonanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.18
trans-2-hexenal
wild type enzyme, at pH 8.0 and 25°C
0.18
trans-2-hexenal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.199
trans-2-hexenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
0.003
trans-2-nonenal
wild type enzyme, at pH 8.0 and 25°C
0.003
trans-2-nonenal
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in 100 mM sodium diphosphate, at pH 8.0 and 22°C
0.0322
trans-2-nonenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
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1.1 - 2.2
trans-2-hexenal
2.7 - 3.8
trans-2-nonenal
8.2
hexanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
11.2
hexanal
wild type enzyme, at pH 8.0 and 25°C
1.8
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
2.2
NAD+
mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
3.1
NAD+
mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
4
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
10.2
NAD+
mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C
10.7
NAD+
mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C
11.4
NAD+
mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.2
NAD+
mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.4
NAD+
mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.7
NAD+
mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C
12.7
NAD+
mutant enzyme E149T/V178R/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
13.1
NAD+
mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
15.7
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
16.3
NAD+
mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
16.6
NAD+
mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C
17.2
NAD+
wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C
18
NAD+
mutant enzyme E149T/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
18.5
NAD+
mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
20.1
NAD+
mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
23.2
NAD+
mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
26.9
NAD+
mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
33.9
NAD+
mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
13
Nonanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
17.9
Nonanal
wild type enzyme, at pH 8.0 and 25°C
1.1
trans-2-hexenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
2.2
trans-2-hexenal
wild type enzyme, at pH 8.0 and 25°C
2.7
trans-2-nonenal
wild type enzyme, at pH 8.0 and 25°C
3.8
trans-2-nonenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
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5.3 - 12.4
trans-2-hexenal
120 - 918
trans-2-nonenal
115
hexanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
154
hexanal
wild type enzyme, at pH 8.0 and 25°C
1.1
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
2.8
NAD+
mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C
3.8
NAD+
mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
4
NAD+
mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C
4.8
NAD+
mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
5
NAD+
mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
5.1
NAD+
mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
6
NAD+
mutant enzyme E149T/V178R/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
6.1
NAD+
mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
6.4
NAD+
mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
6.5
NAD+
mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
8.1
NAD+
mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C
9.5
NAD+
mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
9.9
NAD+
mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C
9.9
NAD+
mutant enzyme E149T/I200V, with nonanal as cosubstrate, at pH 8.0 and 25°C
12.5
NAD+
mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
13.2
NAD+
mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
14.3
NAD+
mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C
24.3
NAD+
mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C
26.3
NAD+
mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C
37.3
NAD+
mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C
40.9
NAD+
wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C
213
Nonanal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
2166
Nonanal
wild type enzyme, at pH 8.0 and 25°C
5.3
trans-2-hexenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
12.4
trans-2-hexenal
wild type enzyme, at pH 8.0 and 25°C
120
trans-2-nonenal
mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C
918
trans-2-nonenal
wild type enzyme, at pH 8.0 and 25°C
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brenda
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UniProt
brenda
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UniProt
brenda
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-
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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isoform ALDH3H1
brenda
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malfunction
the combined disruption of ALDH3I1 and ALDH7B4 decreases the cellular NAD(P)H contents and alters the NAD(P)H/NAD(P)+ ratio. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity and a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type plants. Disruption of ALDH3I1 and ALDH7B4 affects glutathione metabolism and photosynthesis
physiological function
role of ALDHs as major contributors to the homeostasis of pyridine nucleotides in plants
evolution
the enzyme is a member of Arabidopsis thaliana ALDH family 3
evolution
the enzyme is a member of Arabidopsis thaliana ALDH family 7
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AL221_ARATH
596
1
66003
Swiss-Prot
Secretory Pathway (Reliability: 1 )
AL2B4_ARATH
538
0
58589
Swiss-Prot
Mitochondrion (Reliability: 3 )
AL2B7_ARATH
534
0
58153
Swiss-Prot
Mitochondrion (Reliability: 3 )
AL2C4_ARATH
501
0
54360
Swiss-Prot
other Location (Reliability: 3 )
AL3F1_ARATH
484
0
53615
Swiss-Prot
other Location (Reliability: 2 )
AL3H1_ARATH
484
0
53159
Swiss-Prot
other Location (Reliability: 3 )
AL7B4_ARATH
508
0
54208
Swiss-Prot
other Location (Reliability: 3 )
AL3I1_ARATH
550
0
60173
Swiss-Prot
other Location (Reliability: 5 )
A0A178W3F2_ARATH
508
0
54208
TrEMBL
other Location (Reliability: 3 )
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56000
-
2 * 56000, SDS-PAGE
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homodimer
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2 * 56000, SDS-PAGE
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C247S
-
the mutant shows slightly reduced activity compared to the wild type enzyme
C253S
-
the mutation abolishes enzymatic activity
C45S
-
the mutant shows stongly reduced activity compared to the wild type enzyme
E149D
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200V
the mutant shows a good catalysis with NADP+ compared to the wild type enzyme
E149T/V178R/I200V
the mutant uses NADP+ with almost 7fold higher catalytic efficiency compared to NAD+
I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I200G
-
the mutant also exhibits activity with NADP+ and shows decreased affinity for NAD+ compared to the wild type enzyme
I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I200V
-
the mutant also exhibits activity with NADP+ and shows decreased affinity for NAD+ compared to the wild type enzyme
additional information
construction of a single ALDH3I1 mutant K06 line and a double T-DNA insertion mutant line K06/62 that is defective in representative members of Arabidopsis thaliana ALDH families 3 and 7, ALDH3I1 and ALDH7B4, by T-DNA insertion. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
additional information
construction of a single ALDH3I1 mutant K06 line and a double T-DNA insertion mutant line K06/62 that is defective in representative members of Arabidopsis thaliana ALDH families 3 and 7, ALDH3I1 and ALDH7B4, by T-DNA insertion. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
additional information
construction of of a single ALDH7B4 mutant K62 line and a double T-DNA insertion mutant that is defective in representative members of Arabidopsis thaliana ALDH families 3and 7, ALDH3I1 and ALDH7B4, respectively. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant K62 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
additional information
construction of of a single ALDH7B4 mutant K62 line and a double T-DNA insertion mutant that is defective in representative members of Arabidopsis thaliana ALDH families 3and 7, ALDH3I1 and ALDH7B4, respectively. The loss of function of ALDH3I1 and ALDH7B4 leads to a decrease of NAD(P)H, NAD(P)H/NAD(P) ratio, and an alteration of the glutathione pools. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity than the wild-type, indicating a high demand for reduced pyridine nucleotides. Mutant K62 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type. Moreover, the mutant has a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. The levels of the total glutathione (reduced + oxidized) and of the reduced to oxidized glutathione ratio (GSH/GSSG) are reduced by 20% and 33% in KO6/62 compared to wild-type, respectively. Phenotype, overview
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Oxidation leads to a decrease in enzymatic activities to less than 25-35% of the activity of the corresponding reduced form. Reduction of oxidized isoform ALDH3H1 after incubation with 10 mM dithiothreitol for 1 h results in a good recovery of activity to about 83% of the initial activity, but to only 44% after reduction with 10 mM GSH
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724222
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His-tag binding column chromatography
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nickel affinity column chromatography, and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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stress-triggered induction of ALDH3I1
stress-triggered induction of ALDH7B4
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Wei, Y.; Lin, M.; Oliver, D.
The roles of aldehyde dehydrogenases (ALDHs) in the PDH bypass of Arabidopsis
BMC Biochem.
10
7-7
2009
Arabidopsis thaliana
brenda
Stiti, N.; Adewale, I.O.; Petersen, J.; Bartels, D.; Kirch, H.H.
Engineering the nucleotide coenzyme specificity and sulfhydryl redox sensitivity of two stress-responsive aldehyde dehydrogenase isoenzymes of Arabidopsis thaliana
Biochem. J.
434
459-471
2011
Arabidopsis thaliana
brenda
Stiti, N.; Podgorska, K.; Bartels, D.
Aldehyde dehydrogenase enzyme ALDH3H1 from Arabidopsis thaliana: Identification of amino acid residues critical for cofactor specificity
Biochim. Biophys. Acta
1844
681-693
2014
Arabidopsis thaliana (Q70DU8), Arabidopsis thaliana
brenda
Missihoun, T.; Kotchoni, S.; Bartels, D.
Aldehyde dehydrogenases function in the homeostasis of pyridine nucleotides in Arabidopsis thaliana
Sci. Rep.
8
2936
2018
Arabidopsis thaliana (Q8W033), Arabidopsis thaliana (Q9SYG7)
brenda