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Information on EC 1.2.1.22 - lactaldehyde dehydrogenase for references in articles please use BRENDA:EC1.2.1.22
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
ALD,
AldA , ALDH, AvLADH, dehydrogenase, lactaldehyde, L-lactaldehyde dehydrogenase, L-lactaldehyde:NAD oxidoreductase, Lactaldehyde dehydrogenase, LADH, MJ1411,
more
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dehydrogenase, lactaldehyde
-
-
-
-
L-lactaldehyde dehydrogenase
L-lactaldehyde:NAD oxidoreductase
-
-
-
-
Lactaldehyde dehydrogenase
NAD-dependent lactaldehyde dehydrogenase
-
-
nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
-
-
-
-
AvLADH
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-
L-lactaldehyde dehydrogenase
-
-
L-lactaldehyde dehydrogenase
-
-
-
L-lactaldehyde dehydrogenase
-
L-lactaldehyde dehydrogenase
-
-
L-lactaldehyde dehydrogenase
-
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-
L-lactaldehyde dehydrogenase
-
L-lactaldehyde dehydrogenase
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-
L-lactaldehyde dehydrogenase
-
L-lactaldehyde dehydrogenase
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L-lactaldehyde dehydrogenase
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Lactaldehyde dehydrogenase
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Lactaldehyde dehydrogenase
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Lactaldehyde dehydrogenase
-
Lactaldehyde dehydrogenase
-
LADH
-
-
SSO3117
locus name
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(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+
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-
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(S)-lactaldehyde:NAD+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acrylaldehyde + NAD+ + H2O
acrylate + NADH
19% activity compared to D-lactaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
84% activity compared to D-lactaldehyde
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH
97% activity compared to D-lactaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
4% activity compared to D-lactaldehyde
-
-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
L-glyceraldehyde + NAD+ + H2O
L-glycerate + NADH
-
-
-
-
ir
L-lactaldehyde + NAD+ + H2O
L-lactate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH
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-
-
-
ir
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
187% activity compared to D-lactaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
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-
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?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
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ALD wild-type only uses NAD+. F180T mutation renders an enzyme with the ability to use NADP+
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-
?
additional information
?
-
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
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-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
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-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
54% of the activity of L-lactaldehyde
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-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
75% of the activity of (S)-lactaldehyde
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-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
catabolism of L-threonine via amino acetone and methylglyoxal
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-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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essential for catabolism of 1,2-propanediol
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-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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aerobic metabolism of fucose
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(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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general role in aldehyde oxidation, involved in several metabolic pathways
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(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
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ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
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(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
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ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
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(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
best substrate
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-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
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-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
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-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
25% activity compared to D-lactaldehyde
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-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
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56% the rate of L-lactaldehyde reduction
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D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
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?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
0.2% the activity of L-lactaldehyde reduction
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glycolaldehyde + NAD+ + H2O
glycolate + NADH
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glycolaldehyde + NAD+ + H2O
glycolate + NADH
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ir
glycolaldehyde + NAD+ + H2O
glycolate + NADH
35% activity compared to D-lactaldehyde
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?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
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?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
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?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
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?
additional information
?
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oxidizes several aldehydes, e.g. L-glyceraldehyde, glycolaldehyde, methylglyoxal
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additional information
?
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not: acetaldehyde, formaldehyde, propionaldehyde, succinic semialdehyde
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additional information
?
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specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
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additional information
?
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residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification. The wild-type enzyme is not active with D-glyceraldehyde, methylglyoxal, acetaldehyde, L-lactate, or benzaldehyde
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additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
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additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
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additional information
?
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not: acetaldehyde, DL-glyceraldehyde, propionaldehyde, phenylpyruvate
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additional information
?
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specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
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additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
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additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
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(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
additional information
?
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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catabolism of L-threonine via amino acetone and methylglyoxal
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-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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essential for catabolism of 1,2-propanediol
-
-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
aerobic metabolism of fucose
-
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-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
general role in aldehyde oxidation, involved in several metabolic pathways
-
-
-
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
-
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?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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?
additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
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-
additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
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-
additional information
?
-
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
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-
additional information
?
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the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
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NAD+
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NAD+
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four NAD-binding sites per molecule of native enzyme
NAD+
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cofactor flexibility in the constricted active site plays a significant role in the mechanism of oxidation of lactaldehyde to lactate
NAD+
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ALD only uses NAD+. Residue F180 of ALD may participate in coenzyme specificity
NADP+
;
additional information
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NADP+ can not substitute for NAD+
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additional information
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NADP+ can not substitute for NAD+
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additional information
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the negatively charged carboxylate group of E179 destabilizes the binding of the 2'-phosphate group of NADPH sterically and electrostatically, thereby accounting for the lack of enzyme activity with this cofactor
-
additional information
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no activity with NADP+
-
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glyceraldehyde
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substrate inhibition
glycolaldehyde
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substrate inhibition
lactaldehyde
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substrate inhibition
methylglyoxal
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substrate inhibition
Mn2+
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50% inhibition at 10 mM
p-chloromercuribenzoate
-
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p-hydroxymercuribenzoate
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50% inhibition at 1.5 mM
Zn2+
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50% inhibition at 0.4 mM
additional information
-
iodoacetamide, Mn2+, Mg2+, Co2+, no effect at 5 mM
-
Ca2+
-
50% inhibition at 5 mM
Cu2+
-
50% inhibition at 0.25 mM
Cu2+
-
85% inhibition at 0.1 mM
Mg2+
-
56% inhibition at 10 mM
N-ethylmaleimide
-
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dithiothreitol
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slight activation
glutathione
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-
glutathione
-
slight activation
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1.27 - 14.5
(S)-lactaldehyde
15.2
acetaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.15
benzaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.302 - 5.6
D-Lactaldehyde
0.14
glycoaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.15
L-glyceraldehyde
-
-
0.0078
NADP+
-
mutant F180T
4.5
phenylacetaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.24 - 0.284
propionaldehyde
additional information
additional information
-
1.27
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
5.8
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
7.5
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
14.5
(S)-lactaldehyde
-
wild-type, pH 7.0, 37°C
0.302
D-Lactaldehyde
100 mM TES pH 7.5, 2.5 mM NAD+
0.04
L-lactaldehyde
-
-
0.007
NAD+
-
mutant F180T
0.12
NAD+
-
+ L-lactaldehyde
0.28
NAD+
-
cosubstrate glycolaldehyde
0.24
propionaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.25
propionaldehyde
-
wild-type
0.26
propionaldehyde
-
mutant F180T
0.284
propionaldehyde
100 mM TES pH 7.5, 2.5 mM NAD+
additional information
additional information
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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761.5 - 1895
(S)-lactaldehyde
0.6
acetaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.9
benzaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
2
D-Lactaldehyde
100 mM TES pH 7.5, 2.5 mM NAD+
18.3
glycoaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.5
phenylacetaldehyd
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
761.5
(S)-lactaldehyde
-
wild-type, pH 7.0, 37°C
1026
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
1545
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
1895
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
1.8
propionaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
3
propionaldehyde
100 mM TES pH 7.5, 2.5 mM NAD+
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52.5 - 808.1
(S)-lactaldehyde
52.5
(S)-lactaldehyde
-
wild-type, pH 7.0, 37°C
206.1
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
326.8
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
808.1
(S)-lactaldehyde
-
mutant N286H, pH 7.0, 37°C
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0.00048
-
whole cell lysate
0.355
purified recombinant enzyme, S-lactaldehyde, NADP+
0.6
100 mM TES pH 7.5, 2.5 mM NAD+
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
11.5
-
purified recombinant enzyme, glycolaldehyde, NAD+
17.2
-
purified recombinant enzyme, (S)-lactaldehyde, NAD+
2.1
purified recombinant enzyme, R-lactaldehyde, NAD+
2.28
-
purified recombinant enzyme, (R)-D-lactaldehyde, NAD+
3.64
purified recombinant enzyme, S-lactaldehyde, NAD+
4.28
purified recombinant enzyme, glycolaldehyde, NAD+
4.43
purified recombinant enzyme, (R)-lactaldehyde, NAD+
6.95
purified recombinant enzyme, (S)-lactaldehyde, NAD+
8.94
purified recombinant enzyme, glycolaldehyde, NAD+
additional information
-
-
0.00051
-
whole cell lysate
0.00051
-
whole cell lysate, procyclics
0.74
-
wild-type, pH 7.0, 37°C
0.74
-
purified recombinant enzyme, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.18
-
mutant N286H, pH 7.0, 37°C
1.18
-
purified recombinant mutant N286H, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.78
-
mutant N286H, pH 7.0, 37°C
1.78
-
purified recombinant mutant N286E, pH 7.0, 37°C, substrate (S)-lactaldehyde
2.18
-
mutant N286H, pH 7.0, 37°C
2.18
-
purified recombinant mutant N286T, pH 7.0, 37°C, substrate (S)-lactaldehyde
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.
7 - 10
17% activity at pH 7.0, almost 100% activity at pH 10.0
9.2 - 11.2
-
pH 9.2: about 15% of maximum activity, pH 11.2: about 99% of maximum activity
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15
-
recombinant mutant N286H
40
-
recombinant wild-type enzyme
45
-
recombinant mutants N286T and N286E
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
rapid decline in activity above 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
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brenda
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-
brenda
-
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-
brenda
-
SwissProt
brenda
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
brenda
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
brenda
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-
-
brenda
-
-
-
brenda
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-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
constitutive mutant
-
-
brenda
inducible under aerobic conditions
-
-
brenda
lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase are functions of the same protein
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-
brenda
-
-
-
brenda
-
TrEMBL
brenda
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-
-
brenda
additional information
-
no activity in the bloodstream stage of the parasite
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification, molecular structure modeling of wild-type enzyme and N286 mutants
metabolism
the enzyme catalyzes the last step in the degradation of L-fucose
metabolism
-
the enzyme catalyzes the last step in the degradation of L-fucose
-
physiological function
the enzyme catalyzes the last step in the degradation of L-fucose. The activity with L-lactaldehyde is fivefold increased in L-fucose adapted cells compared with D-glucose. Only poor conversion of D-lactaldehyde under both conditions is observed
physiological function
-
the enzyme catalyzes the last step in the degradation of L-fucose. The activity with L-lactaldehyde is fivefold increased in L-fucose adapted cells compared with D-glucose. Only poor conversion of D-lactaldehyde under both conditions is observed
-
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Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
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100000
-
sucrose density gradient centrifugation
40000
-
gel filtration, SDS-PAGE
55000
-
4 * 55000, SDS-PAGE
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?
-
x * 52200, recombinant enzyme, SDS-PAGE
monomer
1 * 55000, SDS-PAGE; 1 * 55000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
calculated from sequence, gel-filtration
tetramer
-
4 * 50000, crystal structure
tetramer
4 * 51000, gel-filtration
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by the hanging-drop, vapor-diffusion method. Serendipitous crystal structure of unliganded lactaldehyde dehydrogenase determined by multiple isomorphous replacement using anomalous scattering, at 2.2 A resolution. Crystal structure of the ternary enzyme complex with products lactate and NADH at 2.1 A resolution, and binary complex complex with NADPH at 2.7 A resolution. The ternary complex reveals that the nicotinamide ring of NADH occupies two distinct conformations, one with the ring positioned in the active site in the so-called hydrolysis conformation and another with the ring extended out of the active site into the solvent region; in complex with NADH and lactate
-
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F180T
-
renders an enzyme with the ability to use NADP+. NADP+ activity is higher than that attained with NAD+. Exhibits a 16fold increase in the Vm/Km ratio with NAD+ as the coenzyme. Absence of Mg2+ inhibitory effect on F180T activity
H449R
-
site-directed mutagenesis
L158Y
-
site-directed mutagenesis
N286A
-
site-directed mutagenesis
N286C
-
site-directed mutagenesis
N286D
-
site-directed mutagenesis
N286F
-
site-directed mutagenesis
N286G
-
site-directed mutagenesis
N286I
-
site-directed mutagenesis
N286K
-
site-directed mutagenesis
N286L
-
site-directed mutagenesis
N286M
-
site-directed mutagenesis
N286P
-
site-directed mutagenesis
N286Q
-
site-directed mutagenesis
N286R
-
site-directed mutagenesis
N286S
-
site-directed mutagenesis
N286V
-
site-directed mutagenesis
N286W
-
site-directed mutagenesis
N286Y
-
site-directed mutagenesis
additional information
-
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
N286E
-
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286E
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal
N286H
-
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
N286T
-
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
N286T
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
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100
25% activity after 100°C for 10 min
40 - 55
-
purified recombinant wild-type enzyme is stable at 40°C after incubation for 1 h, but its stability decreases rapidly above 40°C. The mutants N286E and N286H show the same stability, decreasing rapidly above 40°C and exhibiting 20% and 40% of their maximum activity at 45°C, respectively. In contrast, mutant N286T is stable above 50°C and retains 60% of its maximum activity at 55°C after incubation for 1 h
50
-
pH 6.5, 10 min, 50% loss of activity
55
-
1 h, 70% residual activity for mutant N286T
80
86% activity after 80°C for 10 min
90
45% activity after 90°C for 10 min
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dialysis in absence of EDTA and beta-mercaptoethanol: complete loss of activity
-
purified enzyme is extremely unstable, reactivation with halide ions e.g. Cl-, I-, Br-
-
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-20°C, 100 mM H2NaPO4, pH 7.5, 100 mM NaCl,0.025% 2-mercaptoethanol, 50% glycerol, stable for 6 months
-
-20°C, pH 7.5, purified enzyme is extremely unstable, almost completely inactivated, reactivation with halide ions Cl-, I-, Br-
-
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anion-exchange chromatography
by gel filtration; three chromatography steps
-
mutant F180T purified to homogeneity (more than 95% pure), on Ni2+ resin
-
Ni-affinity chromatography
-
nickel-chelating affinity column
-
nickel-chelating affinity column; nickel-chelating affinity column
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography to near homogeneity
-
-
-
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expression in Escherichia coli
expression in Escherichia coli BL21 as His-tag fusion protein
-
expression in Escherichia coli; heterologous expression with taxadiene synthase in Escherichia coli BL21(DE3)
-
gene aldA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli cells as a His6-tagged enzyme
-
overexpression in Escherichia coli cells as a His6-tagged enzyme; overexpression in Escherichia coli cells as a His6-tagged enzyme
vectors containing His-Tag constructs overexpressed in Escherichia coli BL21 (DE3)pLysS strain
-
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Hacking, A.J.; Lin, E.C.C.
Disruption of the fucose pathway as a consequence of genetic adaptation to propanediol as a carbon source in Escherichia coli
J. Bacteriol.
126
1166-1172
1976
Escherichia coli
brenda
Cocks, G.T.; Aguilar, J.; Lin, E.C.C.
Evolution of L-1,2-propanediol catabolism in Escherichia coli by recruitment of enzymes for L-fucose and L-lactate metabolism
J. Bacteriol.
118
83-88
1974
Escherichia coli
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Caballero, E.; Baldoma, L.; Ros, J.; Boronat, A.; Aguilar, J.
Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli
J. Biol. Chem.
258
7788-7792
1983
Escherichia coli
brenda
Inoue, Y.; Watanabe, K.; Shimosaka, M.; Saikusa, T.; Fukuda, Y.; Murata, K.; Kimura, A.
Metabolism of 2-oxoaldehydes in yeasts. Purification and characterization of lactaldehyde dehydrogenase from Saccharomyces cerevisiae
Eur. J. Biochem.
153
243-247
1985
Saccharomyces cerevisiae
brenda
Baldoma, L.; Aguilar, J.
Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12
J. Biol. Chem.
262
13991-13996
1987
Escherichia coli
brenda
Baldoma, L.; Aguilar, J.
Metabolism of L-fucose and L-rhamnose in Escherichia coli: aerobic-anaerobic regulation of L-lactaldehyde dissimilation
J. Bacteriol.
170
416-421
1988
Escherichia coli
brenda
Sridhara, S.; Wu, T.T.
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli
J. Biol. Chem.
244
5233-5238
1969
Escherichia coli
brenda
Willetts, A.J.; Turner, J.M.
Threonine metabolism in a strain of Bacillus subtilis: enzymic oxidation of the intermediate DL-lactaldehyde
Biochim. Biophys. Acta
222
234-236
1970
Bacillus subtilis
brenda
Rodriguez-Zavala, J.S.; Allali-Hassani, A.; Weiner, H.
Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases
Protein Sci.
15
1387-1396
2006
Escherichia coli
brenda
Grochowski, L.L.; Xu, H.; White, R.H.
Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis
J. Bacteriol.
188
2836-2844
2006
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58806)
brenda
Di Costanzo, L.; Gomez, G.A.; Christianson, D.W.
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity
J. Mol. Biol.
366
481-493
2006
Escherichia coli, Escherichia coli (P25553)
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A comparative study of methylglyoxal metabolism in trypanosomatids
FEBS J.
276
376-386
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Leishmania major, Trypanosoma brucei, Trypanosoma cruzi
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Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase
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17
563-570
2008
Escherichia coli
brenda
Watanabe, S.; Piyanart, S.; Makino, K.
Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway
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275
5139-5149
2008
Azotobacter vinelandii, Azotobacter vinelandii NBRC 102612, Scheffersomyces stipitis (A3LNE3), Scheffersomyces stipitis (A3M013), Scheffersomyces stipitis
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Wu, X.; Xu, L.; Yan, M.
A new NAD(+)-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
Biosci. Biotechnol. Biochem.
80
2306-2310
2016
Escherichia coli, Escherichia coli (P25553)
brenda
Wu, X.; Xu, L.; Yan, M.
A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
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80
2306-2310
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Escherichia coli, Escherichia coli (P25553)
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102
882-908
2016
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