Any feedback?
Information on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.2.1.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.4 aldehyde dehydrogenase (NADP+)Specify your search results
Word Map
- 1.2.1.4
-
voltage-gated
-
kvbeta1
-
voltage-dependent
-
pore-forming
-
juxtaparanodal
-
paranodal
-
caspr
- medicine
- retinaldehyde
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
kvbeta2, aldh6, nadp-dependent aldehyde dehydrogenase, taaldh, aldehyde dehydrogenase (nadp+), aldhpyr1147, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALD6
aldehyde dehydrogenase (NADP+)
aldehyde dehydrogenase 3A1
aldehyde dehydrogenase 6
ALDH
ALDH1F1
ALDH3A1
ALDH6
AlDHPyr1147
dehydrogenase, aldehyde (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
NADP+-dependent Ald6
NADP-acetaldehyde dehydrogenase
-
-
-
-
NADP-dependent aldehyde dehydrogenase
Ta0439
TaAlDH
NADP-dependent aldehyde dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
-
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
-
-
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NADP+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-87-9
-
97162-78-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-cyanobenzaldehyde + NADP+ + H2O
2-cyanobenzoate + NADPH + H+
-
3% activity compared to 4-nitrobenzaldehyde
-
-
?
2-methlybutyraldehyde + NADP+ + H2O
2-methylbutanoate + NADPH + H+
-
16% activity compared to 4-nitrobenzaldehyde
-
-
?
2-nitrobenzaldehyde + NADP+ + H2O
2-nitrobenzoate + NADPH + H+
-
22% activity compared to 4-nitrobenzaldehyde
-
-
?
3-nitrobenzaldehyde + NADP+ + H2O
3-nitrobenzoate + NADPH + H+
-
53% activity compared to 4-nitrobenzaldehyde
-
-
?
4-cyanobenzaldehyde + NADP+ + H2O
4-cyanobenzoate + NADPH + H+
-
6% activity compared to 4-nitrobenzaldehyde
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
20% activity compared to 4-nitrobenzaldehyde
-
-
?
4-nitroacetophenone + NADP+ + H2O
?
-
2% activity compared to 4-nitrobenzaldehyde
-
-
?
4-nitrobenzaldehyde + NADP+ + H2O
4-nitrobenzoate + NADPH + H+
-
100% activity
-
-
?
butanal + NADP+ + H2O
butanoate + NADPH + H+
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
chloroacetaldehyde + NADP+ + H2O
chloroacetate + NADPH + H+
-
most effective substrate in the absence of Mg2+
-
-
?
crotonaldehyde + NADP+ + H2O
crotonate + NADPH + H+
-
2% activity compared to 4-nitrobenzaldehyde
-
-
?
glutaraldehyde + NADP+ + H2O
glutarate + NADPH + H+
-
-
-
-
?
hexanal + NADP+ + H2O
hexanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
isobutanal + NADP+
isobutyrate + NADPH
-
19% of the activity with acetaldehyde
-
-
ir
methylglyoxal + NADP+ + H2O
?
-
7% activity compared to 4-nitrobenzaldehyde
-
-
?
phenylglyoxal + NADP+ + H2O
?
-
3% activity compared to 4-nitrobenzaldehyde
-
-
?
succinic semialdehyde + NADP+ + H2O
?
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
trans,trans-muconaldehyde + NADP+ + H2O
trans,trans-muconic acid + NADPH + H+
-
-
-
?
valeraldehyde + NADP+ + H2O
pentanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+
?
Acetobacter acetigenus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
Gluconobacter gluconicus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
acetate + NADPH + H+
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
131% of the activity with isovaleraldehyde
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
-
l40% of the activity with acetaldehyde
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
-
6% of the activity with isovaleraldehyde
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
8% activity compared to 4-nitrobenzaldehyde
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, enzyme a, b, c, d and e
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, 2% of the activity with acetaldehyde
-
-
ir
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
-
-
-
?
formaldehyde + NADP+
formate + NADPH + H+
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
weak activity with enzyme a, b, d and e
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
low activity
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
low activity
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
2% of the activity with acetaldehyde
-
-
ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
-
ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
-
ir
octanal + NADP+ + H2O
octanoate + NADPH + H+
-
n-octanal, enzyme b, c, d and e
-
-
?
pentanal + NADP+
pentanoate + NADPH
-
n-pentanal, enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
much lower activity than with acetaldehyde
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
102% of the activity with acetaldehyde
-
-
ir
propanal + NADP+ + H2O
propionate + NADPH + H+
-
181% of the activity with isovaleraldehyde
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
enzyme is involved in the oxidation of alkanes
-
-
?
additional information
?
-
-
no activity with glycolaldehyde and glyceraldehyde
-
-
?
additional information
?
-
no activity with phenylacetaldehyde, chlorobenzaldehyde, betaine aldehyde and succinic semialdehyde
-
-
?
additional information
?
-
no activity with phenylacetaldehyde, chlorobenzaldehyde, betaine aldehyde and succinic semialdehyde
-
-
?
additional information
?
-
-
no activity with 4-chlorobenzaldehyde, 4-fluorbenzaldehyde, tolualdehyde, anisaldehyde, formaldehyde, octanal, cinnamaldehyde, and isatin
-
-
?
additional information
?
-
-
enzyme is partly repressed during growth on glucose
-
-
?
additional information
?
-
NADH/formaldehyde detection by luminescence assay using Vibrio fischeri
-
-
-
additional information
?
-
NADH/formaldehyde detection by luminescence assay using Vibrio fischeri
-
-
-
additional information
?
-
no activity with acetaldehyde
-
-
-
additional information
?
-
no activity with acetaldehyde
-
-
-
additional information
?
-
no activity with acetaldehyde
-
-
-
additional information
?
-
no activity with acetaldehyde
-
-
-
additional information
?
-
no activity with acetaldehyde
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NADP+
?
Acetobacter acetigenus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
Gluconobacter gluconicus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
acetate + NADPH + H+
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
-
-
?
formaldehyde + NADP+
formate + NADPH + H+
-
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
enzyme is involved in the oxidation of alkanes
-
-
?
additional information
?
-
-
enzyme is partly repressed during growth on glucose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
reaction with NAD+ is less than 1% of the activity with NADP+
NADP+
the wild-type enzyme strongly prefers NADP+, negligible activity with NAD+
additional information
increased to preferred activity of enzyme mutants with NAD+ compared to NADP+ in contrast to wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
Rb+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in unilamellar liposomes produced by phosphatidylcholine, the enzyme activity decreases to 1% or less of the original activity. About 10% of the original activity can be preserved in unilamellar liposomes prepared from bacterial phospholipids
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Comparative subcellular distribution of benzaldehyde and acetaldehyde dehydrogenase activities in two hepatoma cell lines and in normal hepatocytes.
Carcinoma, Hepatocellular
Oxidative metabolism of 4-hydroxy-2,3-nonenal during diethyl-nitrosamine-induced carcinogenesis in rat liver.
Demyelinating Diseases
Potassium channel distribution, clustering, and function in remyelinating rat axons.
Neoplasms
Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene.
Neoplasms
Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase 6, absent in MCF-7 cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
additional information
additional information
-
Km-values of NADP+ and decanal as a function of the lauryl sarcosin concentration
-
additional information
additional information
-
influence of pH-value and buffer of the Km-value for hexanal
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25
D-glyceraldehyde
pH 7.3, temperature not specified in the publication, wild-type enzyme
3.8
D-glyceraldehyde
pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I
31.2
D-glyceraldehyde
pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I/W271Y/W275V
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00312
-
native enzyme, with NAD+ as cofactor, pH and temperature not specified in the publication
0.00315
-
mutant enzyme A200E, with NAD+ as cofactor, pH and temperature not specified in the publication
0.0113
-
mutant enzyme A200E/V210Q, with NAD+ as cofactor, pH and temperature not specified in the publication
0.012
-
mutant enzyme A200E/V210Q, with NADP+ as cofactor, pH and temperature not specified in the publication
0.06
-
mutant enzyme A200E, with NADP+ as cofactor, pH and temperature not specified in the publication
0.853
-
wild type enzyme from cornea, using propionaldehyde and NAD+ as substrates
3
-
native enzyme, with NADP+ as cofactor, pH and temperature not specified in the publication
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.2
-
pH 5.0: 10% of maximal activity, pH 9.2: 15% of maximal activity
8 - 11.5
-
pH 8.5: about 60% of maximal activity, pH 11.5: about 80% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IFO 3262, IFO 3263, IFO 3264, IFO 3265, IFO 3266, IFO 3267, IFO 3268, IFO 3269, IFO 3270
-
-
brenda
-
1962620 A+, 2159808 A+, 2159809 A+, 2159814 A+, 2159817 A+, 2780956 A+, 2812090 A+, 3469515 A+, 3642329 A+, 3642334 A+, 3642340 A+, 1962620 A++
-
-
amenda
strain ATCC 700926D, highest activity in cells grown with ethanol
-
-
brenda
IFO 3130, IFO 3172, IFO 3289, IFO 3290, IFO 3291, IFO 12528, var. alpha IFO 3254, var. alpha IFO 3255, var. alpha IFO 3256, var. alpha IFO 3257, var. alpha IFO 3258
-
-
brenda
-
-
-
amenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cancerous pneumocytes develop significant higher levels of ALDH3A1 expression than normal pneumocytes
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
physiological function of the regulatory mechanism for NAD+-dependent ALDHs via cysteine oxidation and vicinal disulfide formation using yeast Ald4 (EC 1.2.1.5) and Ald6. While both enzymes convert aldehyde to acetate and are important for yeast ethanol metabolism, they differ in cofactor utilization and the regulatory mechanism. Ald4 prefers NAD+ while Ald6 is NADP+-dependent. The regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction
evolution
-
physiological function of the regulatory mechanism for NAD+-dependent ALDHs via cysteine oxidation and vicinal disulfide formation using yeast Ald4 (EC 1.2.1.5) and Ald6. While both enzymes convert aldehyde to acetate and are important for yeast ethanol metabolism, they differ in cofactor utilization and the regulatory mechanism. Ald4 prefers NAD+ while Ald6 is NADP+-dependent. The regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction
-
metabolism
isozymes Ald4, Ald5 and Ald6 play important roles in yeast survival when using ethanol as the carbon source. Both Ald4 and Ald5 preferentially use NAD+ as cofactors in cells while Ald6 only utilizes NADP+. With ethanol as the carbon source, the pentose phosphate pathway, a major pathway to generate NADPH, is shut down as the substrate is not available
metabolism
-
isozymes Ald4, Ald5 and Ald6 play important roles in yeast survival when using ethanol as the carbon source. Both Ald4 and Ald5 preferentially use NAD+ as cofactors in cells while Ald6 only utilizes NADP+. With ethanol as the carbon source, the pentose phosphate pathway, a major pathway to generate NADPH, is shut down as the substrate is not available
-
physiological function
Ald6 converts aldehyde to acetate and are important for yeast ethanol metabolism Ald6 is utilized as a major pathway for NADPH production. Instead of cysteine, Ald6 has a serine next to the active site cysteine. As the regulatory cysteine inactivates Ald4 during oxidative stress, we hypothesized that under oxidative stress, Ald6 remains active while Ald4 is inactivated, thus diverting all acetaldehyde to Ald6 for the production of NADPH. This way, yeast can survive oxidative stress better
physiological function
-
Ald6 converts aldehyde to acetate and are important for yeast ethanol metabolism Ald6 is utilized as a major pathway for NADPH production. Instead of cysteine, Ald6 has a serine next to the active site cysteine. As the regulatory cysteine inactivates Ald4 during oxidative stress, we hypothesized that under oxidative stress, Ald6 remains active while Ald4 is inactivated, thus diverting all acetaldehyde to Ald6 for the production of NADPH. This way, yeast can survive oxidative stress better
-
additional information
structural modeling and docking, the three-dimensional structure of wild-type TaALDH is modeled using the available crystal structure of the triple mutant TaALDH F34M/Y399C/S405N (PDB ID 5M4X) as a template, molecular dynamics simulations
additional information
-
structural modeling and docking, the three-dimensional structure of wild-type TaALDH is modeled using the available crystal structure of the triple mutant TaALDH F34M/Y399C/S405N (PDB ID 5M4X) as a template, molecular dynamics simulations
-
additional information
-
structural modeling and docking, the three-dimensional structure of wild-type TaALDH is modeled using the available crystal structure of the triple mutant TaALDH F34M/Y399C/S405N (PDB ID 5M4X) as a template, molecular dynamics simulations
-
additional information
-
structural modeling and docking, the three-dimensional structure of wild-type TaALDH is modeled using the available crystal structure of the triple mutant TaALDH F34M/Y399C/S405N (PDB ID 5M4X) as a template, molecular dynamics simulations
-
additional information
-
structural modeling and docking, the three-dimensional structure of wild-type TaALDH is modeled using the available crystal structure of the triple mutant TaALDH F34M/Y399C/S405N (PDB ID 5M4X) as a template, molecular dynamics simulations
-
Show AA Sequence and Transmembrane Helices (1004 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
82000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with isobutyraldehyde and/or NADP+, capillary counterdiffusion method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A200E
-
the mutant shows strongly reduced activity (50fold) with NADP+ compared to the wild type enzyme
A200E/V210Q
-
the mutant shows strongly reduced activity (250fold) with NADP+ and about 3fold increased activity with NAD+ compared to the wild type enzyme
D176S
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K/M262I/W271Y/W275V
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
F34M/Y399C/S405N
site-directed mutagenesis, crystal structure analysis
M262I
site-directed mutagenesis, the mutation results in 30% higher activity with NAD+ compared to wild-type enzyme, the surface mutation M262I has influence on the solubility
S175E
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
additional information
additional information
construction of an enzyme mutant with deletion of the catalytic residues
additional information
-
construction of an enzyme mutant with deletion of the catalytic residues
-
additional information
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-8°C, 16% glycerol, 1 mM dithiothreitol, 12% loss of activity after 6 months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Source 30Q column chromatography and Superdex 200 gel filtration
using a Q-sepharose anion exchange column for enzyme preparation of mouse liver, using nickel agarose affinity chromatography for purification of recombinant protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ALD6, recombinant overexpression of wild-type and mutant GFP-tagged enzymes in Saccharomyces cerevisiae strain MBTL-SYL-1 cytosol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
synthesis
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vandecasteele, J.P.; Guerrillot, L.
Aldehyde dehydrogenases from Pseudomonas aeruginosa
Methods Enzymol.
89
484-490
1982
Pseudomonas aeruginosa
brenda
Guerrillot, L.; Vandecasteele, J.P.
Purification and characterization of two aldehyde dehydrogenases from Pseudomonas aeruginosa
Eur. J. Biochem.
81
185-192
1977
Pseudomonas aeruginosa
brenda
Hommel, R.; Kurth, J.; Kleber, H.P.
NADP+-dependent aldehyde dehydrogenase from Acetobacter rancens CCM 1774: purification and properties
J. Basic Microbiol.
28
25-33
1988
Acetobacter pasteurianus, Acetobacter pasteurianus CCM 1774
-
brenda
Aurich, H.; Sorger, H.; Bergmann, R.; Lasch, J.
Kinetics of membrane-bound aldehyde dehydrogenase from Acinetobacter calcoaceticus
Biol. Chem. Hoppe-Seyler
368
101-109
1987
Acinetobacter calcoaceticus
brenda
Aurich, H.; Sorger, H.; Bergmann, R.; Lasch, J.; Koelsch, R.
Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden. 1. Einflu¯ von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung und Aktivitaet des Enzyms
J. Basic Microbiol.
25
623-629
1985
Acinetobacter calcoaceticus
-
brenda
Aurich, H.; Bergmann, R.; Lasch, J.; Koelsch, R.; Sorger, H.
Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden. 2. Rekonstitution in kuenstlichen Membranvesikeln
J. Basic Microbiol.
25
631-636
1985
Acinetobacter calcoaceticus
-
brenda
Sasaki, S.; Sugawara, Y.
Aldehyde dehydrogenase from Proteus vulgaris
Methods Enzymol.
89
480-483
1982
Proteus vulgaris
brenda
Muraoka, H.; Watabe, Y.; Ogasawara, N.; Takahashi, H.
Purification and properties of five NADP-dependent aldehyde dehydrogenases from Acetobacter aceti
J. Ferment. Technol.
58
501-507
1980
Acetobacter aceti
-
brenda
Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
Crystallization and properties of NADP-dependent aldehyde dehydrogenase from Gluconobacter melanogenus
Agric. Biol. Chem.
44
155-164
1980
Acetobacter aceti, Acetobacter acetigenus, Acetobacter orleanensis, Acetobacter ascendens, Frateuria aurantia, Gluconobacter oxydans, Acetobacter pasteurianus, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconacetobacter liquefaciens, Gluconobacter roseus, Gluconobacter sphaericus
-
brenda
Sugawara, Y.; Sasaki, S.
Purification and properties of aldehyde dehydrogenase from Proteus vulgaris
Biochim. Biophys. Acta
480
343-350
1977
BRENDA: Proteus vulgaris
Textmining: Phaseolus vulgaris
brendaamenda
amenda
Seegmiller, J.E.
Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast
J. Biol. Chem.
201
629-637
1953
Saccharomyces cerevisiae
brenda
Jacobson, M.K.; Bernofsky, C.
Mitochondrial acetaldehyde dehydrogenase from Saccharomyces cerevisiae
Biochim. Biophys. Acta
350
277-291
1974
Saccharomyces cerevisiae
brenda
Dickinson, F.M.
The purification and some properties of the Mg(2+)-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae
Biochem. J.
315
393-399
1996
Saccharomyces cerevisiae
brenda
Ho, K.K.; Weiner, H.
Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli
J. Bacteriol.
187
1067-1073
2005
Escherichia coli
brenda
Estey, T.; Piatigorsky, J.; Lassen, N.; Vasiliou, V.
ALDH3A1: a corneal crystallin with diverse functions
Exp. Eye Res.
84
3-12
2007
Oryctolagus cuniculus, Homo sapiens, Mammalia, Mus musculus
brenda
Short, D.M.; Lyon, R.; Watson, D.G.; Barski, O.A.; McGarvie, G.; Ellis, E.M.
Metabolism of trans, trans-muconaldehyde, acytotoxic metabolite of benzene, in mouse liver by alcohol dehydrogenase Adh1 and aldehyde reductase AKR1A4
Toxicol. Appl. Pharmacol.
210
163-170
2006
Mus musculus (Q540D7)
brenda
Lassen, N.; Bateman, J.B.; Estey, T.; Kuszak, J.R.; Nees, D.W.; Piatigorsky, J.; Duester, G.; Day, B.J.; Huang, J.; Hines, L.M.; Vasiliou, V.
Multiple and additive functions of ALDH3A1 and ALDH1A1: cataract phenotype and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice
J. Biol. Chem.
282
25668-25676
2007
Mus musculus
brenda
Patel, M.; Lu, L.; Zander, D.S.; Sreerama, L.; Coco, D.; Moreb, J.S.
ALDH1A1 and ALDH3A1 expression in lung cancers: correlation with histologic type and potential precursors
Lung Cancer
59
340-349
2008
Homo sapiens
brenda
Alka, K.; Ryan, B.J.; Dolly, J.O.; Henehan, G.T.
Substrate profiling and aldehyde dismutase activity of the Kvbeta2 subunit of the mammalian Kv1 potassium channel
Int. J. Biochem. Cell Biol.
42
2012-2018
2010
Rattus norvegicus
brenda
Mihasan, M.; Stefan, M.; Hritcu, L.; Artenie, V.; Brandsch, R.
Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1
Res. Microbiol.
164
22-30
2013
Paenarthrobacter nicotinovorans
brenda
Mukhopadhyay, A.; Wei, B.; Weiner, H.
Mitochondrial NAD dependent aldehyde dehydrogenase either from yeast or human replaces yeast cytoplasmic NADP dependent aldehyde dehydrogenase for the aerobic growth of yeast on ethanol
Biochim. Biophys. Acta
1830
3391-3398
2013
BRENDA: Saccharomyces cerevisiae
Textmining: Homo sapiens
brendaamenda
amenda
Bezsudnova, E.Y.; Petrova, T.E.; Artemova, N.V.; Boyko, K.M.; Shabalin, I.G.; Rakitina, T.V.; Polyakov, K.M.; Popov, V.O.
NADP-dependent aldehyde dehydrogenase from archaeon Pyrobaculum sp.1860: structural and functional features
Archaea
2016
9127857
2016
BRENDA: Pyrobaculum ferrireducens (G7VCG0), Pyrobaculum ferrireducens 1860 (G7VCG0)
Textmining: archaeon
brendaamenda
amenda
Zhang, Y.; Wang, M.; Lin, H.
A regulatory cysteine residue mediates reversible inactivation of NAD+-dependent aldehyde dehydrogenases to promote oxidative stress response
ACS Chem. Biol.
15
28-32
2020
Saccharomyces cerevisiae (P54115), Saccharomyces cerevisiae ATCC 204508 (P54115)
brenda
Gmelch, T.J.; Sperl, J.M.; Sieber, V.
Molecular dynamics analysis of a rationally designed aldehyde dehydrogenase gives insights into improved activity for the non-native cofactor NAD
ACS Synth. Biol.
9
920-929
2020
Thermoplasma acidophilum (Q9HL01), Thermoplasma acidophilum AMRC-C165 (Q9HL01), Thermoplasma acidophilum ATCC 25905 (Q9HL01), Thermoplasma acidophilum JCM 9062 (Q9HL01), Thermoplasma acidophilum NBRC 15155 (Q9HL01)
brenda
Lee, S.; Park, D.J.; Yoon, J.; Bang, S.H.; Kim, Y.H.; Min, J.
Formaldehyde treatment using overexpressed aldehyde dehydrogenase 6 from recombinant Saccharomyces cerevisiae
J. Nanosci. Nanotechnol.
18
2979-2985
2018
Saccharomyces cerevisiae (P54115), Saccharomyces cerevisiae ATCC 204508 (P54115)
brenda
Hsu, LC; Chang, WC; Hiraoka, L; Hsieh, CL
Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6.
Genomics
24
333-41
1994
Homo sapiens
amenda
Riveros-Rosas, H; Julián-Sánchez, A; Moreno-Hagelsieb, G; Muñoz-Clares, RA
Aldehyde dehydrogenase diversity in bacteria of the Pseudomonas genus.
Chem Biol Interact
304
83-87
2019
Pseudomonas
amenda
Rexer, BN; Zheng, WL; Ong, DE
Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase 6, absent in MCF-7 cells.
Cancer Res
61
7065-70
2001
Homo sapiens, Transformation
amenda
Mic, FA; Molotkov, A; Fan, X; Cuenca, AE; Duester, G
RALDH3, a retinaldehyde dehydrogenase that generates retinoic acid, is expressed in the ventral retina, otic vesicle and olfactory pit during mouse development.
Mech Dev
97
227-30
2000
Mus musculus, Homo sapiens
amenda
Cobessi, D; Tête-Favier, F; Marchal, S; Azza, S; Branlant, G; Aubry, A
Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
J Mol Biol
290
161-73
1999
Streptococcus mutans
amenda
Cobessi, D; Tête-Favier, F; Marchal, S; Branlant, G; Aubry, A
Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
J Mol Biol
300
141-52
2000
Streptococcus mutans
amenda
Marchal, S; Cobessi, D; Rahuel-Clermont, S; Tête-Favier, F; Aubry, A; Branlant, G
Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Chem Biol Interact
130-132
15-28
2001
Streptococcus mutans
amenda
Lazaroff, MA; Taylor, AD; Ribera, AB
In vivo analysis of Kvbeta2 function in Xenopus embryonic myocytes.
J Physiol
541
673-83
2002
Xenopus
amenda
Van Urk, H; Voll, WS; Scheffers, WA; Van Dijken, JP
Transient-State Analysis of Metabolic Fluxes in Crabtree-Positive and Crabtree-Negative Yeasts.
Appl Environ Microbiol
56
281-287
1990
yeasts, Saccharomyces cerevisiae
amenda
Hasegawa, M; Asanuma, S; Fujiyuki, T; Kiya, T; Sasaki, T; Endo, D; Morioka, M; Kubo, T
Differential gene expression in the mandibular glands of queen and worker honeybees, Apis mellifera L.: Implications for caste-selective aldehyde and fatty acid metabolism.
Insect Biochem Mol Biol
39
661-7
2009
Apis mellifera
amenda
Niegemann, E; Schulz, A; Bartsch, K
Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene.
Arch Microbiol
160
454-60
1993
Rattus, Mammalia, Aspergillus nidulans, Escherichia coli, Saccharomyces cerevisiae
amenda
Li, H; Wagner, E; McCaffery, P; Smith, D; Andreadis, A; Dräger, UC
A retinoic acid synthesizing enzyme in ventral retina and telencephalon of the embryonic mouse.
Mech Dev
95
283-9
2000
Mus musculus, Homo sapiens
amenda
Walter, RD; Ebert, F
Evidence for NADH- and NADPH-linked glutamate dehydrogenases in Trypanosoma cruzi epimastigotes.
J Protozool
26
653-6
1979
Trypanosoma cruzi
amenda
Rasband, MN; Trimmer, JS; Schwarz, TL; Levinson, SR; Ellisman, MH; Schachner, M; Shrager, P
Potassium channel distribution, clustering, and function in remyelinating rat axons.
J Neurosci
18
36-47
1998
Rattus
amenda
Accili, EA; Kuryshev, YA; Wible, BA; Brown, AM
Separable effects of human Kvbeta1.2 N- and C-termini on inactivation and expression of human Kv1.4.
J Physiol
512 ( Pt 2)
325-36
1998
Homo sapiens, Rattus
amenda
McCormack, T; McCormack, K; Nadal, MS; Vieira, E; Ozaita, A; Rudy, B
The effects of Shaker beta-subunits on the human lymphocyte K+ channel Kv1.3.
J Biol Chem
274
20123-6
1999
Homo sapiens, Mus musculus, Mus sp.
amenda
Monaghan, MM; Trimmer, JS; Rhodes, KJ
Experimental localization of Kv1 family voltage-gated K+ channel alpha and beta subunits in rat hippocampal formation.
J Neurosci
21
5973-83
2001
Rattus, Hippocampus
amenda
Wang, X; Zhang, J; Berkowski, SM; Knowleg, H; Chandramouly, AB; Downens, M; Prystowsky, MB
Protein kinase C-mediated phosphorylation of Kv beta 2 in adult rat brain.
Neurochem Res
29
1879-86
2004
Rattus
amenda
Leoni, AL; Marionneau, C; Demolombe, S; Le Bouter, S; Mangoni, ME; Escande, D; Charpentier, F
Chronic heart rate reduction remodels ion channel transcripts in the mouse sinoatrial node but not in the ventricle.
Physiol Genomics
24
4-12
2005
Mus sp.
amenda
Grün, F; Hirose, Y; Kawauchi, S; Ogura, T; Umesono, K
Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase prominently expressed in sensory neuroepithelia during development.
J Biol Chem
275
41210-8
2000
Mus musculus
amenda
Ferro, M; Muzio, G; Bassi, AM; Biocca, ME; Canuto, RA
Comparative subcellular distribution of benzaldehyde and acetaldehyde dehydrogenase activities in two hepatoma cell lines and in normal hepatocytes.
Cell Biochem Funct
9
149-54
1991
Rattus
amenda
Rhodes, KJ; Strassle, BW; Monaghan, MM; Bekele-Arcuri, Z; Matos, MF; Trimmer, JS
Association and colocalization of the Kvbeta1 and Kvbeta2 beta-subunits with Kv1 alpha-subunits in mammalian brain K+ channel complexes.
J Neurosci
17
8246-58
1997
Rattus
amenda
Tipparaju, SM; Barski, OA; Srivastava, S; Bhatnagar, A
Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel.
Biochemistry
47
8840-54
2008
Rattus
amenda
González-Segura, L; Riveros-Rosas, H; Díaz-Sánchez, AG; Julián-Sánchez, A; Muñoz-Clares, RA
Potential monovalent cation-binding sites in aldehyde dehydrogenases.
Chem Biol Interact
202
41-50
2013
Bacillales, animal
amenda
Downen, M; Belkowski, S; Knowles, H; Cardillo, M; Prystowsky, MB
Developmental expression of voltage-gated potassium channel beta subunits.
Brain Res Dev Brain Res
117
71-80
1999
Mus musculus
amenda
Rasband, MN; Trimmer, JS; Peles, E; Levinson, SR; Shrager, P
K+ channel distribution and clustering in developing and hypomyelinated axons of the optic nerve.
J Neurocytol
28
319-31
0
Rattus
amenda
McCormack, K; Connor, JX; Zhou, L; Ho, LL; Ganetzky, B; Chiu, SY; Messing, A
Genetic analysis of the mammalian K+ channel beta subunit Kvbeta 2 (Kcnab2).
J Biol Chem
277
13219-28
2002
Mus sp.
amenda
Grande, M; Suà rez, E; Vicente, R; Cantó, C; Coma, M; Tamkun, MM; Zorzano, A; Gumà , A; Felipe, A
Voltage-dependent K+ channel beta subunits in muscle: differential regulation during postnatal development and myogenesis.
J Cell Physiol
195
187-93
2003
Rattus
amenda
Pineda, RH; Knoeckel, CS; Taylor, AD; Estrada-Bernal, A; Ribera, AB
Kv1 Potassium Channel Complexes In Vivo Require Kv{beta}2 Subunits in Dorsal Spinal Neurons.
J Neurophysiol
100
2125-36
2008
Xenopus
amenda
Barski, OA; Tipparaju, SM; Bhatnagar, A
Kinetics of nucleotide binding to the beta-subunit (AKR6A2) of the voltage-gated potassium (Kv) channel.
Chem Biol Interact
178
165-70
2009
Rattus
amenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.2.1.4)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
