Information on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+] and Organism(s) Homo sapiens and UniProt Accession P47895

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This record set is specific for:
Homo sapiens
UNIPROT: P47895


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
1.2.1.5
-
RECOMMENDED NAME
GeneOntology No.
aldehyde dehydrogenase [NAD(P)+]
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tryptophan degradation V (side chain pathway)
-
-
tryptophan metabolism
-
-
Glycolysis / Gluconeogenesis
-
-
Histidine metabolism
-
-
Tyrosine metabolism
-
-
Phenylalanine metabolism
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beta-Alanine metabolism
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Metabolism of xenobiotics by cytochrome P450
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Drug metabolism - cytochrome P450
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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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-
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-88-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
isotype ALDH1A1 is the key ALDH isozyme linked to tissue stem cells populations and an important contributor to cancer stem cells function in cancers
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
show the reaction diagram
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
show the reaction diagram
preferred substrate of isozyme ALDH1A3
-
-
?
1-formyl-6-methylpyrene + NADP+ + H2O
6-methylpyrene-1-carboxylic acid + NADPH + H+
show the reaction diagram
-
-
-
?
1-formyl-8-methylpyrene + NADP+ + H2O
8-methylpyrene-1-carboxylic acid + NADPH + H+
show the reaction diagram
-
-
-
?
1-formylpyrene + NADP+ + H2O
pyrene-1-carboxylic acid + NADPH + H+
show the reaction diagram
-
-
-
?
2-formylpyrene + NADP+ + H2O
pyrene-2-carboxylic acid + NADPH + H+
show the reaction diagram
-
-
-
?
2-naphthaldehyde + NADH + H+
2-naphthyl alcohol + NAD+
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
show the reaction diagram
-
-
-
?
4-formylpyrene + NADP+ + H2O
pyrene-4-carboxylic acid + NADPH + H+
show the reaction diagram
-
-
-
?
4-pyridinecarboxaldehyde + NAD+ + H2O
4-pyridinecarboxylate + NADH + H+
show the reaction diagram
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NADH + H+
6-methoxy-2-naphthyl alcohol + NAD+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
show the reaction diagram
aldophosphamide + NAD+
N,N-bis-(2-chloroethyl)-diaminophosphoric-(2-carboxyethylester) + ?
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
show the reaction diagram
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
show the reaction diagram
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
show the reaction diagram
-
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
show the reaction diagram
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
mafosfamide + NADP+ + H2O
?
show the reaction diagram
-
-
-
-
?
malondialdehyde + NAD+
? + NADH
show the reaction diagram
-
no activity
-
-
-
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
p-hydroxybenzaldehyde + NADP+ + H2O
p-hydroxybenzoic acid + NADPH + H+
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NADP+ + H2O
p-nitrobenzoate + NADPH + H+
show the reaction diagram
-
-
-
-
?
propanal + 1,N6-ethenoadenine dinucleotide
propionate + ?
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + 3-acetylpyridine adenine dinucleotide
propionate + ?
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + 3-pyridine adenine dinucleotide
propionate + ?
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
show the reaction diagram
propanal + beta-NADP+ + H2O
propionate + beta-NADPH + H+
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + N-guanine dinucleotide
propionate + ?
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + N-hypoxanthine dinucleotide
propionate + ?
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
show the reaction diagram
-
-
-
?
trans-2-hexenal + NAD+
trans-2-hexenoate + NADH
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
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
-
-
NAD+
required
NAD(P)+
-
-
NADH
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
stimulatory effect at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Disulfiram
0.01 mM
3-thionicotinamide adenine dinucleotide
-
strong inhibition versus beta-NAD+, isoenzyme E2; substrate inhibition, isoenzyme E1
beta-NADP+
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substrate inhibition, isoenzyme E1
dimethyl ampal thiolester
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complete inhibition of isozyme ALDH3 at 0.0075 mM
Disulfiram
0.01 mM
methyl ampal thiolester
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78% inhibition of isozyme ALDH3 at 0.0075 mM
p-hydroxymercuribenzoate
-
0.05 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
-
0.05 mM, 1.8fold stimulation
H2O2
-
0.015 mM, 1.2fold stimulation
Sodium dodecyl sulfate
-
0.01 mM, 1.1fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 0.015
3,4-dihydroxyphenylacetaldehyde
0.096
1,N6-ethenoadenine dinucleotide
-
isoenzyme E2
0.0016
1-formyl-6-methylpyrene
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ALDH3A1, at pH 7.5 and 37°C
0.004
1-formyl-8-methylpyrene
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ALDH3A1,at pH 7.5 and 37°C
0.004
1-formylpyrene
-
ALDH3A1, at pH 7.5 and 37°C
0.011
2-formylpyrene
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ALDH3A1, at pH 7.5 and 37°C
0.0007
2-naphthaldehyde
-
pH 7.5, 25°C
0.015
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH3A1
0.0132 - 0.62
3-acetylpyridine adenine dinucleotide
0.0338 - 0.504
3-pyridinealdehyde adenine dinucleotide
0.0151
3-thionicotinamide adenine dinucleotide
-
isoenzyme E1
0.00078
4-formylpyrene
-
ALDH3A1, at pH 7.5 and 37°C
0.091 - 0.19
4-Pyridinecarboxaldehyde
0.0033
6-methoxy-2-naphthaldehyde
-
pH 7.5, 25°C
67 - 81
acetaldehyde
0.64
aldophosphamide
-
reaction with NAD+
0.148 - 0.64
benzaldehyde
0.0047
beta-NAD+
-
-
7.68
beta-NADP+
-
isoenzyme E1
0.094
betaNAD+
-
isoenzyme E2
0.013 - 0.46
Chloroacetaldehyde
0.0053
cinnamaldehyde
-
pH 7.5, 25°C
0.06
Hexanal
-
-
0.0113
N-1,N6-ethenoadenine dinucleotide
-
isoenzyme E1
1.33
N-guanine dinucleotide
-
isoenzyme E1
0.121 - 1.36
N-hypoxanthine dinucleotide
0.032 - 2.1
NAD+
0.49 - 1
NADP+
0.067 - 0.113
octanal
19 - 19.06
propanal
12
propionaldehyde
-
ALDH3A1, at pH 7.5 and 37°C
0.1
trans-2-hexenal
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35.9
acetaldehyde
-
-
51
benzaldehyde
-
-
0.47 - 7.7
Chloroacetaldehyde
34
Hexanal
-
-
0.47 - 45.3
NAD+
38.8
NADP+
-
reaction with benzaldehyde
53
trans-2-hexenal
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5 - 200
Chloroacetaldehyde
1.8 - 158.3
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16.67
-
enzyme from breast adenocarcinoma cell line
32.95
-
enzyme from stomach mucosa
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
benzaldehyde oxidation, enzyme from breast adenocarcinoma cell line
8 - 9
-
benzaldehyde oxidation, enzyme from stomach mucosa
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
P47895
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000, enzyme from breast adenocarcinoma cell line, SDS-PAGE
54500
-
2 * 54500, enzyme from stomach mucosa, SDS-PAGE
55000
-
4 * 55000, SDS-PAGE
108000
-
enzyme from stomach mucosa, gel filtration
110000
-
non-denaturing PAGE
125000
-
enzyme from breast adenocarcinoma cell line, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 40000, enzyme from breast adenocarcinoma cell line, SDS-PAGE; 2 * 54500, enzyme from stomach mucosa, SDS-PAGE
homotetramer
-
4 * 55000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the apoenzyme is crystallized by using 100 mM ACES, pH 6.4, 100-200 mM guanidine-HCl, 1-10 mM MgCl2 and 16–17% (w/v) PEG 6000, the mutant T244A in complex with NAD is crystallized by using 100 mM ACES, pH 6.4, 100 mM guanidine–HCl, 10 mM MgCl2 and 18% (w/v) PEG 6000
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
highest stability of enzyme from breast adenocarcinoma cell line
348784
7.4
-
the activity at a physiological pH value (7.4) is nearly 50% of the activity observed at the optimal pH value
684721
7.5 - 9.5
-
highest stability of enzyme from stomach mucosa
348784
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
2 h, 34% residual activity
50
-
7 min, almost complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing, more than once causes complete loss of activity of enzyme from breast adenocarcinoma cell line, enzyme from stomach mucosa retains 40% of its activity even after being frozen and thawed eight times
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.5, 25 mM sodium phosphate supplemented with 1 mM EDTA and 0.05% dithiothreitol, 10% glycerol, enzyme from breast adenocarcinoma cell line completely loses activity after 15 days, enzyme from stomach mucosa loses 75% of its activity after 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE MacroPrep column chromatography
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DEAE-cellulose column chromatography, 5’-AMP Sepharose 4B and 4-hydroxyacetophenone affinity chromatography
-
nickel affinity column chromatography
-
single-step purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli XL-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aldehyde dehydrogenase 1A3 is transcriptionally activated by 0.001 mM all-trans-retinoic acid in human epidermal keratinocytes whereas no upregulation is detected in dermal fibroblasts and HeLa cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T186S
-
the mutant has increased activity against aldehyde and decreased activity against smaller substrates like benzaldehyde compared to the native enzyme and cells transformed with the point mutant are better protected against the killing effect of cyclophosphamides
T244A
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244G
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244S
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244V
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine