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Information on EC 1.2.1.22 - lactaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.22
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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 enzyme appears in viruses and cellular organisms
- 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, nad-dependent lactaldehyde dehydrogenase, nicotinamide adenine dinucleotide (nad)-linked dehydrogenase, mj1411, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldA
AN0544
AvLADH
dehydrogenase, lactaldehyde
-
-
-
-
L-lactaldehyde dehydrogenase
L-lactaldehyde:NAD oxidoreductase
-
-
-
-
Lactaldehyde dehydrogenase
LADH
nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
-
-
-
-
SSO3117
additional information
Lactaldehyde dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 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 + 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
?
-
-
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+
-
-
-
?
(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 + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
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+
-
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
-
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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
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
-
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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
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+
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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
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 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
-
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
-
metabolism
Aspergillus nidulans NRRL 194
-
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
a loss-of-function mutation severely impairs L-rhamnose utilization
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
-
a loss-of-function mutation severely impairs L-rhamnose utilization
-
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
Show AA Sequence and Transmembrane Helices (1351 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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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
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
-
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
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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
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
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced on L-rhamnose via the transcriptional activator RhaR. The relative contribution of RhaR to the induction of aldA is the same as that for its induction of the LraA-LraC and rhamnosidase genes
expression is induced on L-rhamnose via the transcriptional activator RhaR. The relative contribution of RhaR to the induction of aldA is the same as that for its induction of the LraA-LraC and rhamnosidase genes
expression is induced on L-rhamnose via the transcriptional activator RhaR. The relative contribution of RhaR to the induction of aldA is the same as that for its induction of the LraA-LraC and rhamnosidase genes
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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.
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
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
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.
2021
2420-2432
2021
Aspergillus nidulans (A0A1U8QKS3), Aspergillus nidulans, Aspergillus nidulans ATCC 38163 (A0A1U8QKS3)
brenda
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