Information on EC 1.2.1.3 - aldehyde dehydrogenase (NAD+) and Organism(s) Arabidopsis thaliana

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This record set is specific for:
Arabidopsis thaliana


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


The taxonomic range for the selected organisms is: Arabidopsis thaliana

EC NUMBER
COMMENTARY hide
1.2.1.3
-
RECOMMENDED NAME
GeneOntology No.
aldehyde dehydrogenase (NAD+)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alkane oxidation
-
-
aromatic biogenic amine degradation (bacteria)
-
-
ethanol degradation III
-
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
-
dimethylsulfoniopropanoate biosynthesis II (Spartina)
-
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serotonin degradation
-
-
dimethylsulfoniopropanoate biosynthesis I (Wollastonia)
-
-
fatty acid alpha-oxidation I
-
-
fatty acid alpha-oxidation II
-
-
hypotaurine degradation
-
-
ethanol degradation IV
-
-
L-tryptophan degradation X (mammalian, via tryptamine)
-
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NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)
-
-
fatty acid alpha-oxidation III
-
-
noradrenaline and adrenaline degradation
-
-
histamine degradation
-
-
phytol degradation
-
-
dopamine degradation
-
-
putrescine degradation III
-
-
ethanol degradation II
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octane oxidation
-
-
alanine metabolism
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-
Entner Doudoroff pathway
-
-
histidine metabolism
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-
non-pathway related
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octane oxidation
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propanol degradation
-
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Glycolysis / Gluconeogenesis
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-
Ascorbate and aldarate metabolism
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-
Fatty acid degradation
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Valine, leucine and isoleucine degradation
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Lysine degradation
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Arginine and proline metabolism
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Histidine metabolism
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Tryptophan metabolism
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beta-Alanine metabolism
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Glycerolipid metabolism
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Pyruvate metabolism
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Chloroalkane and chloroalkene degradation
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Limonene and pinene degradation
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Insect hormone biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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-
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD+ oxidoreductase
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-86-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-hydroxynonenal + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
dodecanal + NAD+ + H2O
dodecanoate + NADH + H+
show the reaction diagram
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
nonanal + NAD+ + H2O
nonanoate + NADH + H+
show the reaction diagram
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
trans-2-hexenal + NAD+ + H2O
(E)-hex-2-enoate + NADH + H+
show the reaction diagram
trans-2-nonenal + NAD+ + H2O
(E)-non-2-enoate + NADH + H+
show the reaction diagram
-
-
-
?
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
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0403
4-hydroxynonenal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22C
0.005
dodecanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22C
0.071 - 0.072
Hexanal
0.119 - 4.136
NAD+
0.008 - 0.065
Nonanal
0.029
octanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22C
0.51
propionaldehyde
-
in 100 mM sodium diphosphate, at pH 8.0 and 22C
0.18 - 0.199
trans-2-hexenal
0.003 - 0.0322
trans-2-nonenal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.2 - 11.2
Hexanal
1.8 - 33.9
NAD+
13 - 17.9
Nonanal
1.1 - 2.2
trans-2-hexenal
2.7 - 3.8
trans-2-nonenal
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
115 - 154
Hexanal
1.1 - 40.9
NAD+
213 - 2166
Nonanal
5.3 - 12.4
trans-2-hexenal
120 - 918
trans-2-nonenal
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
2 * 56000, SDS-PAGE
112000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 56000, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
724222
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tag binding column chromatography
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nickel affinity column chromatography, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+