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

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EC Tree
IUBMB Comments
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aldh2, aldh1, aldh1a1, aldehyde dehydrogenase 2, aldh1a3, aldh3a1, aldehyde dehydrogenase 1, aldh1a2, mitochondrial aldehyde dehydrogenase, aldehyde dehydrogenase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AHD-M1
-
-
-
-
ALDDH
-
-
-
-
Aldehyde dehydrogenase [NAD+]
-
-
-
-
Aldehyde dehydrogenase, cytosolic
-
-
-
-
Aldehyde dehydrogenase, microsomal
-
-
-
-
aldehyde:NAD+ oxidoreductase
-
-
-
-
ALDH-E1
-
-
-
-
ALDH-E2
-
-
-
-
ALDH1
-
-
-
-
ALDH1-NL
-
-
-
-
ALDH3H1
ALDHI
-
-
-
-
ALDHX
-
-
-
-
ALHDII
-
-
-
-
Allergen Alt a 10
-
-
-
-
Brassica turgor-responsive/drought-induced gene 26 protein
-
-
-
-
Btg-26
-
-
-
-
CoA-independent aldehyde dehydrogenase
-
-
-
-
ETA-crystallin
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
-
-
-
-
K(+)-ACDH
-
-
-
-
K(+)-activated acetaldehyde dehydrogenase
-
-
-
-
m-methylbenzaldehyde dehydrogenase
-
-
-
-
Matured fruit 60 kDa protein
-
-
-
-
MF-60
-
-
-
-
Mg(2+)-ACDH
-
-
-
-
Mg(2+)-activated acetaldehyde dehydrogenase
-
-
-
-
NAD+-linked aldehyde dehydrogenase
-
-
-
-
NAD-aldehyde dehydrogenase
-
-
-
-
NAD-dependent 4-hydroxynonenal dehydrogenase
-
-
-
-
NAD-dependent aldehyde dehydrogenase
-
-
-
-
NAD-linked aldehyde dehydrogenase
-
-
-
-
Non-lens ALDH1
-
-
-
-
P51
-
-
-
-
PM-ALDH9
-
-
-
-
propionaldehyde dehydrogenase
-
-
-
-
R-aminobutyraldehyde dehydrogenase
-
-
-
-
RALDH
-
-
-
-
RALDH(II)
-
-
-
-
RalDH1
-
-
-
-
Retinal dehydrogenase
-
-
-
-
Turgor-responsive protein 26G
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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
-
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 SUBSTRATE
NATURAL PRODUCT
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 22°C
0.005
dodecanal
-
in 100 mM sodium diphosphate, at pH 8.0 and 22°C
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 22°C
0.51
propionaldehyde
-
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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112000
-
gel filtration
56000
-
2 * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 56000, SDS-PAGE
PROTEIN VARIANTS
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+
I200G
I200V
additional information
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
-
nickel affinity column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stress-triggered induction of ALDH3I1
stress-triggered induction of ALDH7B4
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team