show all | hide all No of entries

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

for references in articles please use BRENDA:EC1.2.1.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P47895 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
acetaldehyde dehydrogenase, aldh3, aldh1a, class 3 aldehyde dehydrogenase, myo-inositol dehydrogenase, aldh9, tumor-associated aldehyde dehydrogenase, aldh2a, osaldh7, aldh3i1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde dehydrogenase
247
-
aldehyde dehydrogenase 1A3
284066
isoform
ALDH1
247
-
ALDH1A1
247
isotype
Aldh1a3
ALDH2
247
-
ALDH3
ALDH3A1
284062
-
Aldh3b1
284067
-
ALDHIII
-
-
-
-
BCP54
-
-
-
-
class 3 aldehyde dehydrogenase
284062
-
Corneal 15.8 kDa protein
-
-
-
-
Corneal protein 54
-
-
-
-
dehydrogenase, aldehyde (nicotinamide adenine dinucleotide (phosphate))
-
-
-
-
HTC-ALDH
-
-
-
-
Transparentin
-
-
-
-
Tumor-associated aldehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-88-0
-
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 + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
-
?
propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
show the reaction diagram
-
isoenzyme E1 and E2
-
-
?
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 SUBSTRATE
NATURAL PRODUCT
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
-
-
-
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
INHIBITOR
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+
-
substrate inhibition, isoenzyme E1
dimethyl ampal thiolester
-
complete inhibition of isozyme ALDH3 at 0.0075 mM
Disulfiram
0.01 mM
methyl ampal thiolester
-
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
-
ALDH3A1, at pH 7.5 and 37°C
0.004
1-formyl-8-methylpyrene
-
ALDH3A1,at pH 7.5 and 37°C
0.004
1-formylpyrene
-
ALDH3A1, at pH 7.5 and 37°C
0.011
2-formylpyrene
-
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
0.032 - 2.1
NAD+
0.49 - 1
NADP+
0.067 - 0.113
octanal
0.121 - 1.36
oxidized nicotinamide hypoxanthine dinucleotide
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
AL1A3_HUMAN
512
0
56108
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
SUBUNIT
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
-
PROTEIN VARIANTS
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
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Izaguirre, G.; Pietruszko, R.; Cho, S.; MacKerell, A.D., Jr.
Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs
J. Biomol. Struct. Dyn.
19
429-447
2001
Homo sapiens
Manually annotated by BRENDA team
King, G.; Holmes, R.S.
Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic variation
Biochem. Mol. Biol. Int.
31
49-63
1993
Homo sapiens
Manually annotated by BRENDA team
Sreerama, L.; Sladek, N.E.
Identification and characterization of a novel class 3 aldehyde dehydrogenase overexpressed in a human breast adenocarcinoma cell line exhibiting oxazaphosphorine-specific acquired resistance
Biochem. Pharmacol.
45
2487-2505
1993
Homo sapiens
Manually annotated by BRENDA team
Glatt, H.; Rost, K.; Frank, H.; Seidel, A.; Kollock, R.
Detoxification of promutagenic aldehydes derived from methylpyrenes by human aldehyde dehydrogenases ALDH2 and ALDH3A1
Arch. Biochem. Biophys.
477
196-205
2008
Homo sapiens (P30838)
Manually annotated by BRENDA team
Ho, K.K.; Mukhopadhyay, A.; Li, Y.F.; Mukhopadhyay, S.; Weiner, H.
A point mutation produced a class 3 aldehyde dehydrogenase with increased protective ability against the killing effect of cyclophosphamide
Biochem. Pharmacol.
76
690-696
2008
Homo sapiens, Homo sapiens (P30838)
Manually annotated by BRENDA team
Quash, G.; Fournet, G.; Courvoisier, C.; Martinez, R.M.; Chantepie, J.; Paret, M.J.; Pharaboz, J.; Joly-Pharaboz, M.O.; Gore, J.; Andre, J.; Reichert, U.
Aldehyde dehydrogenase inhibitors: alpha,beta-acetylenic N-substituted aminothiolesters are reversible growth inhibitors of normal epithelial but irreversible apoptogens for cancer epithelial cells from human prostate in culture
Eur. J. Med. Chem.
43
906-916
2008
Homo sapiens, Homo sapiens (P30838)
Manually annotated by BRENDA team
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens (P30838), Homo sapiens (P43353), Homo sapiens (P47895)
Manually annotated by BRENDA team
Marchitti, S.A.; Brocker, C.; Stagos, D.; Vasiliou, V.
Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily
Expert. Opin. Drug Metab. Toxicol.
4
697-720
2008
Homo sapiens
Manually annotated by BRENDA team
Koenig, U.; Amatschek, S.; Mildner, M.; Eckhart, L.; Tschachler, E.
Aldehyde dehydrogenase 1A3 is transcriptionally activated by all-trans-retinoic acid in human epidermal keratinocytes
Biochem. Biophys. Res. Commun.
400
207-211
2010
Homo sapiens (P47895)
Manually annotated by BRENDA team
Gonzalez-Segura, L.; Ho, K.K.; Perez-Miller, S.; Weiner, H.; Hurley, T.D.
Catalytic contribution of threonine 244 in human ALDH2
Chem. Biol. Interact.
202
32-40
2013
Homo sapiens
Manually annotated by BRENDA team
Alam, M.F.; Laskar, A.A.; Choudhary, H.H.; Younus, H.
Human salivary aldehyde dehydrogenase: purification, kinetic characterization and effect of ethanol, hydrogen peroxide and sodium dodecyl sulfate on the activity of the enzyme
Cell Biochem. Biophys.
74
307-315
2016
Homo sapiens (P30838)
Manually annotated by BRENDA team
Tomita, H.; Tanaka, K.; Tanaka, T.; Hara, A.
Aldehyde dehydrogenase 1A1 in stem cells and cancer
Oncotarget
7
11018-11032
2016
Homo sapiens
Manually annotated by BRENDA team
Select items on the left to see more content.