Any feedback?
No. of entries
Information on EC 1.2.1.22 - lactaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.22 lactaldehyde dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.2.1.22
- aldolase
- l-lactate
- l-rhamnose
- glycol
- l-fucose
- dehydrogenases
- 1-phosphate
- methylglyoxal
- glycolaldehyde
-
nad+-dependent
- l-1,2-propanediol
-
propanediol
-
non-phosphorylated
-
permease
-
dissimilate
- dihydroxyacetone
showSynonyms
lactaldehyde dehydrogenase, l-lactaldehyde dehydrogenase, psladh, avladh, mj1411, nad-dependent lactaldehyde dehydrogenase, nicotinamide adenine dinucleotide (nad)-linked dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldA
aldehyde dehyrogenase
AN0544
AvLADH
dehydrogenase, lactaldehyde
-
-
-
-
L-lactaldehyde dehydrogenase
L-lactaldehyde:NAD oxidoreductase
-
-
-
-
Lactaldehyde dehydrogenase
LADH
nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
-
-
-
-
SSO3117
Lactaldehyde 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
(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-lactaldehyde degradation (aerobic), L-rhamnose degradation II, lactate biosynthesis (archaea), methylglyoxal degradation V
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-lactaldehyde:NAD+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-90-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
Substrates: -
Products: -
Products: -
?
acrylaldehyde + NAD+ + H2O
acrylate + NADH
Substrates: 19% activity compared to D-lactaldehyde
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
Substrates: 84% activity compared to D-lactaldehyde
Products: -
Products: -
?
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH
Substrates: 97% activity compared to D-lactaldehyde
Products: -
Products: -
?
formaldehyde + NAD+ + H2O
formate + NADH
Substrates: 4% activity compared to D-lactaldehyde
Products: -
Products: -
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-glyceraldehyde + NAD+ + H2O
L-glycerate + NADH
-
Substrates: -
Products: -
Products: -
ir
L-lactaldehyde + NAD+ + H2O
L-lactate + NADH + H+
Substrates: -
Products: -
Products: -
?
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH
Substrates: 187% activity compared to D-lactaldehyde
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
Substrates: ALD wild-type only uses NAD+. F180T mutation renders an enzyme with the ability to use NADP+
Products: -
Products: -
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
Substrates: 8.6% of the activity of (S)-lactaldehyde
Products: -
Products: -
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
Substrates: 8.6% of the activity of (S)-lactaldehyde
Products: -
Products: -
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
Substrates: 75% of the activity of (S)-lactaldehyde
Products: -
Products: -
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
Substrates: 54% of the activity of L-lactaldehyde
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: catabolism of L-threonine via amino acetone and methylglyoxal
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: essential for catabolism of 1,2-propanediol
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: aerobic metabolism of fucose
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: general role in aldehyde oxidation, involved in several metabolic pathways
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans CBS 112.46
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans M139
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans NRRL 194
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: best substrate
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: best substrate
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
Substrates: best substrate
Products: -
Products: -
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
Substrates: assay using NADP+
Products: -
Products: -
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
Substrates: assay using NADP+
Products: -
Products: -
?
acetaldehyde + NAD+
acetate + NADH + H+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+
acetate + NADH + H+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+
acetate + NADH + H+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: 25% activity compared to D-lactaldehyde
Products: -
Products: -
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
Substrates: 56% the rate of L-lactaldehyde reduction
Products: -
Products: -
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
Substrates: -
Products: -
Products: -
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
Substrates: 0.2% the activity of L-lactaldehyde reduction
Products: -
Products: -
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
Substrates: 35% activity compared to D-lactaldehyde
Products: -
Products: -
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: oxidizes several aldehydes, e.g. L-glyceraldehyde, glycolaldehyde, methylglyoxal
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: acetaldehyde, formaldehyde, propionaldehyde, succinic semialdehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: acetaldehyde, DL-glyceraldehyde, propionaldehyde, phenylpyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: catabolism of L-threonine via amino acetone and methylglyoxal
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: essential for catabolism of 1,2-propanediol
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: aerobic metabolism of fucose
Products: -
Products: -
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
Substrates: general role in aldehyde oxidation, involved in several metabolic pathways
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans CBS 112.46
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans M139
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Aspergillus nidulans NRRL 194
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
ALD only uses NAD+. Residue F180 of ALD may participate in coenzyme specificity
NAD+
cofactor flexibility in the constricted active site plays a significant role in the mechanism of oxidation of lactaldehyde to lactate
additional information
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
-
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
-
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
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
-
iodoacetamide, Mn2+, Mg2+, Co2+, no effect at 5 mM
-
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.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
0.14
glycoaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
4.5
phenylacetaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.24
propionaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
additional information
additional information
Michaelis-Menten kinetics
-
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
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+
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+
1.8
propionaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
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.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00051
0.355
purified recombinant enzyme, S-lactaldehyde, NADP+
0.74
purified recombinant enzyme, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.18
purified recombinant mutant N286H, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
1.78
purified recombinant mutant N286E, pH 7.0, 37°C, substrate (S)-lactaldehyde
2.18
purified recombinant mutant N286T, pH 7.0, 37°C, substrate (S)-lactaldehyde
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+
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
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
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.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
brenda
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
brenda
lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase are functions of the same protein
-
-
brenda
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
additional information
-
no activity in the bloodstream stage of the parasite
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme catalyzes the last step in the degradation of L-fucose
metabolism
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
metabolism
-
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
-
metabolism
-
the enzyme catalyzes the last step in the degradation of L-fucose
-
metabolism
-
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
-
metabolism
Aspergillus nidulans CBS 112.46
-
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
-
metabolism
Aspergillus nidulans NRRL 194
-
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
-
metabolism
Aspergillus nidulans M139
-
the enzyme is involved in the non-phosphoryating L-rhamnose catabolic pathway
-
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
-
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LADH_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
465
0
50803
Swiss-Prot
-
LADH_META3
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
465
0
51327
Swiss-Prot
-
LADH_METVS
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
465
0
51019
Swiss-Prot
Mitochondrion (Reliability: 1)
LADH_METM7
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
465
0
51010
Swiss-Prot
-
LADH_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
463
0
51136
Swiss-Prot
-
LADH_METMP
Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
465
0
50981
Swiss-Prot
-
A0A076LB92_9EURY
463
0
51397
TrEMBL
-
A0A126QYI8_METOL
471
0
50573
TrEMBL
other Location (Reliability: 4)
A0A166E4G6_9EURY
470
0
50761
TrEMBL
-
A0A1H7KLH5_9EURY
470
0
50419
TrEMBL
-
A0A1V6N1B5_METAZ
470
0
50875
TrEMBL
-
A0A2L1CBJ1_METMI
465
0
51030
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2U1S8Y2_9EURY
468
0
50156
TrEMBL
other Location (Reliability: 2)
A0A2Z5PRH2_METMI
465
0
51078
TrEMBL
other Location (Reliability: 4)
A0A315XNL1_9EURY
470
0
50445
TrEMBL
Secretory Pathway (Reliability: 4)
A0A328PDR2_9EURY
469
0
51244
TrEMBL
Secretory Pathway (Reliability: 2)
A0A366MDA4_9EURY
470
0
51060
TrEMBL
other Location (Reliability: 5)
A0A3N5AZI5_9EURY
470
0
50418
TrEMBL
-
A0A7J4MUU3_METTF
470
0
50429
TrEMBL
-
A0A7J9P2V7_METMI
465
0
50981
TrEMBL
other Location (Reliability: 1)
A0A7J9S3H0_METMI
465
0
51063
TrEMBL
Mitochondrion (Reliability: 4)
A0A833A778_9EURY
420
0
45860
TrEMBL
Secretory Pathway (Reliability: 1)
A0A832ZJI5_9EURY
466
0
51506
TrEMBL
Mitochondrion (Reliability: 5)
A0A833DRR5_9EURY
468
0
50996
TrEMBL
-
A0A833EAT5_9EURY
466
0
51538
TrEMBL
-
A0A842YQK0_METTF
470
0
50309
TrEMBL
-
A0A843AQQ4_METAZ
470
0
50875
TrEMBL
-
A0A843AWE8_METFO
468
0
50252
TrEMBL
other Location (Reliability: 2)
A0A8D6SWW5_9EURY
463
0
51282
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8T5UYP7_9EURY
468
0
50237
TrEMBL
-
A0A8T8K3C4_9EURY
470
0
50855
TrEMBL
-
A0A9E7UG32_METWO
470
0
50501
TrEMBL
Secretory Pathway (Reliability: 1)
A5UKE4_METS3
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)
470
0
50652
TrEMBL
other Location (Reliability: 4)
A9A9H7_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
465
0
50903
TrEMBL
-
C7P994_METFA
Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
463
0
51177
TrEMBL
-
C9RGC0_METVM
Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
463
0
51112
TrEMBL
-
D3E1W2_METRM
Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)
471
0
50745
TrEMBL
-
D5VRF7_METIM
Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)
447
0
49886
TrEMBL
-
D7DQZ5_METV3
Methanococcus voltae (strain ATCC BAA-1334 / A3)
468
0
51578
TrEMBL
-
D9PXK2_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
470
0
50763
TrEMBL
-
E3GYW0_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
468
0
51064
TrEMBL
-
F6BCN3_METIK
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5)
463
0
50796
TrEMBL
Secretory Pathway (Reliability: 1)
F6D6D7_METPW
Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1)
468
0
50447
TrEMBL
Secretory Pathway (Reliability: 3)
F8AMR6_METOI
Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1)
465
0
50939
TrEMBL
-
K2RSS0_METFP
Methanobacterium formicicum (strain DSM 3637 / PP1)
468
0
50362
TrEMBL
-
O27059_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
455
0
48826
TrEMBL
other Location (Reliability: 4)
A3LNE3_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
495
0
53490
TrEMBL
-
A3M013_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
501
0
54133
TrEMBL
-
Q5BFY6_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
173
0
20094
TrEMBL
-
KGSDH_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
478
0
52290
Swiss-Prot
-
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
55000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
additional information
additional information
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
additional information
-
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-chelating affinity column
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography to near homogeneity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene aldA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene AN0544 or aldA, DNA and amino acid sequence determination and analysis, genetic organization
heterologous expression with taxadiene synthase in Escherichia coli BL21(DE3)
overexpression in Escherichia coli cells as a His6-tagged enzyme
vectors containing His-Tag constructs overexpressed in Escherichia coli BL21 (DE3)pLysS strain
-
overexpression in Escherichia coli cells as a His6-tagged enzyme
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
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
brenda
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 (Q58806), Methanocaldococcus jannaschii
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 (P25553), Escherichia coli
brenda
Greig, N.; Wyllie, S.; Patterson, S.; Fairlamb, A.H.
A comparative study of methylglyoxal metabolism in trypanosomatids
FEBS J.
276
376-386
2009
Leishmania major, Trypanosoma brucei, Trypanosoma cruzi
brenda
Rodriguez-Zavala, J.S.
Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase
Protein Sci.
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
FEBS J.
275
5139-5149
2008
Azotobacter vinelandii, Azotobacter vinelandii NBRC 102612, Scheffersomyces stipitis, Scheffersomyces stipitis (A3LNE3), Scheffersomyces stipitis (A3M013)
brenda
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 (P25553), Escherichia coli
brenda
Wolf, J.; Stark, H.; Fafenrot, K.; Albersmeier, A.; Pham, T.K.; Mueller, K.B.; Meyer, B.H.; Hoffmann, L.; Shen, L.; Albaum, S.P.; Kouril, T.; Schmidt-Hohagen, K.; Neumann-Schaal, M.; Braesen, C.; Kalinowski, J.; Wright, P.C.; Albers, S.V.; Schomburg, D.; Siebers, B.
A systems biology approach reveals major metabolic changes in the thermoacidophilic archaeon Sulfolobus solfataricus in response to the carbon source L-fucose versus D-glucose
Mol. Microbiol.
102
882-908
2016
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
brenda
MacCabe, A.; Sanmartin, G.; Orejas, M.
Identification of the genes encoding the catalytic steps corresponding to LRA4 (l-2-keto-3-deoxyrhamnonate aldolase) and L-lactaldehyde dehydrogenase in Aspergillus nidulans evidence for involvement of the loci AN9425/lraD and AN0544/aldA in the L-rhamnose catabolic pathway
Environ. Microbiol.
23
2420-2432
2021
Aspergillus nidulans (Q5BFY6), Aspergillus nidulans, Aspergillus nidulans ATCC 38163 (Q5BFY6), Aspergillus nidulans CBS 112.46 (Q5BFY6), Aspergillus nidulans FGSC A4 (Q5BFY6), Aspergillus nidulans M139 (Q5BFY6), Aspergillus nidulans NRRL 194 (Q5BFY6)
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.1.22)
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 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
