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Enzyme Nomenclature
Information on EC 1.2.1.22 - lactaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.22
Word Map on EC 1.2.1.22
- 1.2.1.22
-
aldolase
- l-lactate
- l-rhamnose
- glycol
-
1-phosphate
- l-fucose
-
nad+-dependent
- l-1,2-propanediol
- methylglyoxal
-
propanediol
- glycolaldehyde
- dihydroxyacetone
-
dehydratase
- pentose
-
dissimilate
-
permease
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.22
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RECOMMENDED NAME
GeneOntology No.
lactaldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-90-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase are functions of the same protein
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
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
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the enzyme catalyzes the last step in the degradation of L-fucose
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
-
-
-
?
acrylaldehyde + NAD+ + H2O
acrylate + NADH
19% activity compared to D-lactaldehyde
-
-
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
84% activity compared to D-lactaldehyde
-
-
?
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH
97% activity compared to D-lactaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
4% activity compared to D-lactaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
187% activity compared to D-lactaldehyde
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
ALD wild-type only uses NAD+. F180T mutation renders an enzyme with the ability to use NADP+
-
-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
-
-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
-
-
?
(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
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
catabolism of L-threonine via amino acetone and methylglyoxal
-
-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
essential for catabolism of 1,2-propanediol
-
-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
aerobic metabolism of fucose
-
-
-
(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+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
-
-
-
-
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
best substrate
-
-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
-
-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
25% activity compared to D-lactaldehyde
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
56% the rate of L-lactaldehyde reduction
-
-
-
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
0.2% the activity of L-lactaldehyde reduction
-
-
-
glycolaldehyde + NAD+ + H2O
glycolate + NADH
35% activity compared to D-lactaldehyde
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
-
-
?
additional information
?
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-
oxidizes several aldehydes, e.g. L-glyceraldehyde, glycolaldehyde, methylglyoxal
-
-
-
additional information
?
-
-
not: acetaldehyde, formaldehyde, propionaldehyde, succinic semialdehyde
-
-
-
additional information
?
-
-
specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
-
-
-
additional information
?
-
-
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
-
-
-
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+
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
A3LNE3, A3M013
-
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
catabolism of L-threonine via amino acetone and methylglyoxal
-
-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
essential for catabolism of 1,2-propanediol
-
-
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
aerobic metabolism of fucose
-
-
-
(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+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Q97UA1
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
Q97UA1
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
cofactor flexibility in the constricted active site plays a significant role in the mechanism of oxidation of lactaldehyde to lactate
NAD+
-
ALD only uses NAD+. Residue F180 of ALD may participate in coenzyme specificity
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
iodoacetamide, Mn2+, Mg2+, Co2+, no effect at 5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
phenaylacetaldehyd
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
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0.24
propionaldehyde
-
100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
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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
phenaylacetaldehyd
-
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+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00051
0.355
purified recombinant enzyme, S-lactaldehyde, NADP+
0.74
1.18
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
1.78
2.1
purified recombinant enzyme, R-lactaldehyde, NAD+
2.18
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+
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
1.78
-
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
no activity in the bloodstream stage of the parasite
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
Q58806
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
Q58806
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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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; in complex with NADH and lactate
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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-
-
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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-
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
vectors containing His-Tag constructs overexpressed in Escherichia coli BL21 (DE3)pLysS strain
-
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ENGINEERING
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
N286H
N286T
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.22)
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