HOME
login
history
all enzymes
BRENDA home
History
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
- l-fucose
- glycol
-
1-phosphate
-
propanediol
- l-1,2-propanediol
- methylglyoxal
-
nad+-dependent
- glycolaldehyde
-
dissimilate
-
permease
-
dehydratase
- pentose
- dihydroxyacetone
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.2.1.22
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
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
BRENDA Link
KEGG Link
MetaCyc Link
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.
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.
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
-
-
Please 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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
(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
?
-
-
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
-
-
-
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
?
-
-
not: acetaldehyde, DL-glyceraldehyde, propionaldehyde, phenylpyruvate
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
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+
-
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
-
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.
INHIBITORS
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
phenaylacetaldehyd
-
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+
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
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+
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
1.18
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
1.78
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
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.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
no activity in the bloodstream stage of the parasite
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
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.
SUBUNITS
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; in complex with NADH and lactate
-
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; 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; 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.22)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
