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Information on EC 1.2.1.22 - lactaldehyde dehydrogenase
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EC Tree
1.2.1.22 lactaldehyde dehydrogenaseSpecify your search results
Word Map
- 1.2.1.22
- aldolase
- l-lactate
- l-rhamnose
- glycol
- dehydrogenases
- 1-phosphate
- l-fucose
- glycolaldehyde
-
nad+-dependent
- l-1,2-propanediol
- methylglyoxal
-
propanediol
- dehydratase
-
permease
- dihydroxyacetone
-
dissimilate
- pentose
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ALD, AldA, ALDH, AvLADH, dehydrogenase, lactaldehyde, L-lactaldehyde dehydrogenase, L-lactaldehyde:NAD oxidoreductase, Lactaldehyde dehydrogenase, LADH, MJ1411, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldA
AvLADH
dehydrogenase, lactaldehyde
-
-
-
-
L-lactaldehyde dehydrogenase
L-lactaldehyde:NAD oxidoreductase
-
-
-
-
Lactaldehyde dehydrogenase
LADH
nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
-
-
-
-
SSO3117
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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
-
-
-
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NATURAL SUBSTRATE
NATURAL 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+
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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INHIBITOR
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+
-
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
2.18
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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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
no activity in the bloodstream stage of the parasite
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
-
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
-
Show AA Sequence and Transmembrane Helices (1188 entries)
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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)
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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNIT
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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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
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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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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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.
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Escherichia coli
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Grochowski, L.L.; Xu, H.; White, R.H.
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Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58806)
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Di Costanzo, L.; Gomez, G.A.; Christianson, D.W.
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity
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Escherichia coli, Escherichia coli (P25553)
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Greig, N.; Wyllie, S.; Patterson, S.; Fairlamb, A.H.
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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.
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Watanabe, S.; Piyanart, S.; Makino, K.
Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway
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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.
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Escherichia coli, Escherichia coli (P25553)
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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.
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2306-2310
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Escherichia coli, Escherichia coli (P25553)
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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.
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882-908
2016
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
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