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Information on EC 1.2.1.22 - lactaldehyde dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P25553
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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
- l-fucose
- dehydrogenases
- 1-phosphate
- methylglyoxal
- glycolaldehyde
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nad+-dependent
- l-1,2-propanediol
-
propanediol
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non-phosphorylated
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permease
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dissimilate
- dihydroxyacetone
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lactaldehyde dehydrogenase, l-lactaldehyde dehydrogenase, psladh, avladh, nad-dependent lactaldehyde dehydrogenase, nicotinamide adenine dinucleotide (nad)-linked dehydrogenase, mj1411, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, lactaldehyde
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L-lactaldehyde:NAD oxidoreductase
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Lactaldehyde dehydrogenase
nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
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Lactaldehyde dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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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
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
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ALD wild-type only uses NAD+. F180T mutation renders an enzyme with the ability to use NADP+
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-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
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-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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essential for catabolism of 1,2-propanediol
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?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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aerobic metabolism of fucose
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-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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general role in aldehyde oxidation, involved in several metabolic pathways
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-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
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?
additional information
?
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residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification. The wild-type enzyme is not active with D-glyceraldehyde, methylglyoxal, acetaldehyde, L-lactate, or benzaldehyde
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-
?
additional information
?
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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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oxidizes several aldehydes, e.g. L-glyceraldehyde, glycolaldehyde, methylglyoxal
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?
additional information
?
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not: acetaldehyde, formaldehyde, propionaldehyde, succinic semialdehyde
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?
additional information
?
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specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
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-
?
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+
(S)-lactate + NADH
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essential for catabolism of 1,2-propanediol
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?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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aerobic metabolism of fucose
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
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general role in aldehyde oxidation, involved in several metabolic pathways
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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+
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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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additional information
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the negatively charged carboxylate group of E179 destabilizes the binding of the 2'-phosphate group of NADPH sterically and electrostatically, thereby accounting for the lack of enzyme activity with this cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.2
acetaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.15
benzaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.14
glycoaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
4.5
phenylacetaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.24
propionaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
additional information
additional information
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
acetaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.9
benzaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
18.3
glycoaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.5
phenylacetaldehyd
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
1.8
propionaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.74
1.18
1.78
2.18
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2 - 11.2
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pH 9.2: about 15% of maximum activity, pH 11.2: about 99% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N286E
N286H
N286T
F180T
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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
additional information
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
additional information
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
additional information
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calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis in absence of EDTA and beta-mercaptoethanol: complete loss of activity
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aldA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
heterologous expression with taxadiene synthase in Escherichia coli BL21(DE3)
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
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
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
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
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
Sridhara, S.; Wu, T.T.
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli
J. Biol. Chem.
244
5233-5238
1969
Escherichia coli
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
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
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
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
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