Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-hydroperoxycyclophosphamide + NADP+
?
-
low activity
-
-
?
4-hydroxy-2-nonenal + NADP+
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
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
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NADP+
acetate + NADPH
-
-
-
-
?
acetaldehyde + NADP+
acetate + NADPH + H+
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
benzaldehyde + NADP+
benzoate + NADPH
benzaldehyde + NADP+
benzoate + NADPH + H+
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
butanal + NADP+ + H2O
butanoate + NADPH + H+
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
-
?
butyraldehyde + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
chloroacetaldehyde + NADP+ + H2O
chloroacetate + NADPH + H+
-
most effective substrate in the absence of Mg2+
-
-
?
crotonaldehyde + NADP+
crotonate + NADPH
-
weak, enzyme a, b and c
-
-
?
crotonaldehyde + NADP+ + H2O
crotonate + NADPH + H+
-
2% activity compared to 4-nitrobenzaldehyde
-
-
?
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
decanal + NADP+
decanoate + NADPH
dodecanal + NADP+ + H2O
dodecanoate + NADPH + H+
-
-
-
-
?
formaldehyde + NAD+
formate + NADH + H+
formaldehyde + NADP+
formate + NADPH + H+
formaldehyde + NADP+ + H2O
formate + NADPH + H+
glutaraldehyde + NADP+ + H2O
glutarate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+
glycerate + NADPH
-
weak, enzyme a, b and d
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
-
-
-
?
heptanal + NADP+
heptanoate + NADPH
hexanal + NADP+
hexanoate + NADPH
hexanal + NADP+ + H2O
hexanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
isobutanal + NADP+
isobutyrate + NADPH
-
19% of the activity with acetaldehyde
-
-
ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
isopentanal + NADP+ + H2O
isopentanoate + NADPH + H+
-
-
-
-
?
mafosfamide + NADP+
?
-
low activity
-
-
?
malondialdehyde + NADP+
?
-
poor substrate
-
-
?
methylglyoxal + NADP+ + H2O
?
-
7% activity compared to 4-nitrobenzaldehyde
-
-
?
nonanal + NAD+ + H2O
nonanoate + NADH + H+
-
-
-
-
r
nonanal + NADP+ + H2O
nonanoate + NADPH + H+
-
-
-
-
r
octanal + NADP+ + H2O
octanoate + NADPH + H+
pentanal + NADP+
pentanoate + NADPH
phenylglyoxal + NADP+ + H2O
?
-
3% activity compared to 4-nitrobenzaldehyde
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
propionaldehyde + NADP+
propionate + NADPH + H+
-
poor substrate
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
succinic semialdehyde + NADP+ + H2O
?
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
tetradecanal + NADP+
tetradecanoate + NADPH
-
-
-
-
?
trans,trans-muconaldehyde + NADP+ + H2O
trans,trans-muconic acid + NADPH + H+
-
-
-
?
trans-2-hexenal + NADP+ + H2O
(2E)-hex-2-enoate + NADPH + H+
trans-2-nonenal + NADP+ + H2O
(2E)-non-2-enoate + NADPH + H+
trans-2-octenal + NADP+ + H2O
(2E)-oct-2-enoate + NADPH + H+
tridecanal + NADP+
tridecanoate + NADPH
-
-
-
-
?
undecanal + NADP+
undecanoate + NADPH
-
-
-
-
?
valeraldehyde + NADP+ + H2O
pentanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
additional information
?
-
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+
-
-
-
-
?
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+
acetate + NADPH + H+
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Acetobacter acetigenus
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Gluconobacter gluconicus
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?, ir
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
131% of the activity with isovaleraldehyde
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
-
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
-
enzyme b and e
-
-
?
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+
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
8% activity compared to 4-nitrobenzaldehyde
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, enzyme a, b, c, d and e
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, 2% of the activity with acetaldehyde
-
-
ir
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
-
-
-
?
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+
-
-
-
?
D-glyceraldehyde + NADP+
D-glycerate + NADPH + H+
-
-
-
?
decanal + NADP+
decanoate + NADPH
-
-
-
-
?
decanal + NADP+
decanoate + NADPH
-
-
-
-
?
formaldehyde + NAD+
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+
formate + NADH + H+
-
-
-
?
formaldehyde + NADP+
formate + 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+
-
-
-
-
?
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
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
heptanal + NADP+
heptanoate + NADPH
-
n-heptanal, enzyme b, c and e
-
-
?
heptanal + NADP+
heptanoate + NADPH
-
-
-
-
?
heptanal + NADP+
heptanoate + NADPH
-
-
-
-
?
hexanal + NADP+
hexanoate + NADPH
-
-
-
-
?
hexanal + NADP+
hexanoate + NADPH
-
-
-
-
?
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
-
-
?
octanal + NADP+ + H2O
octanoate + NADPH + H+
-
-
-
-
?
octanal + NADP+ + H2O
octanoate + NADPH + H+
-
-
-
-
?
pentanal + NADP+
pentanoate + NADPH
-
n-pentanal, enzyme a, b, c, d and e
-
-
?
pentanal + NADP+
pentanoate + NADPH
-
-
-
-
?
pentanal + NADP+
pentanoate + NADPH
-
-
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
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
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
trans-2-hexenal + NADP+ + H2O
(2E)-hex-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-hexenal + NADP+ + H2O
(2E)-hex-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-hexenal + NADP+ + H2O
(2E)-hex-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-hexenal + NADP+ + H2O
(2E)-hex-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-nonenal + NADP+ + H2O
(2E)-non-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-nonenal + NADP+ + H2O
(2E)-non-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-nonenal + NADP+ + H2O
(2E)-non-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-nonenal + NADP+ + H2O
(2E)-non-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-octenal + NADP+ + H2O
(2E)-oct-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-octenal + NADP+ + H2O
(2E)-oct-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-octenal + NADP+ + H2O
(2E)-oct-2-enoate + NADPH + H+
-
-
-
-
?
trans-2-octenal + NADP+ + H2O
(2E)-oct-2-enoate + 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
?
-
-
inducible enzyme
-
-
?
additional information
?
-
-
inducible enzyme
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
R197E
-
very low activity
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
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Proteus vulgaris
brenda
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
Saccharomyces cerevisiae
brenda
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
Pyrobaculum ferrireducens (G7VCG0), Pyrobaculum ferrireducens 1860 (G7VCG0)
brenda
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