Information on EC 1.2.1.22 - lactaldehyde dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.2.1.22
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RECOMMENDED NAME
GeneOntology No.
lactaldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lactaldehyde degradation (aerobic)
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L-rhamnose degradation II
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lactate biosynthesis (archaea)
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methylglyoxal degradation V
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L-lactaldehyde degradation
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Pyruvate metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-90-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; strain NBRC 102612
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Manually annotated by BRENDA team
strain NBRC 102612
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
show the reaction diagram
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
show the reaction diagram
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-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
show the reaction diagram
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
show the reaction diagram
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
acrylaldehyde + NAD+ + H2O
acrylate + NADH
show the reaction diagram
19% activity compared to D-lactaldehyde
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-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
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-
-
-
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
show the reaction diagram
84% activity compared to D-lactaldehyde
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-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
show the reaction diagram
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH
show the reaction diagram
97% activity compared to D-lactaldehyde
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-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
4% activity compared to D-lactaldehyde
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-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH + H+
show the reaction diagram
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-
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-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
show the reaction diagram
L-glyceraldehyde + NAD+ + H2O
L-glycerate + NADH
show the reaction diagram
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-
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ir
L-lactaldehyde + NAD+ + H2O
L-lactate + NADH + H+
show the reaction diagram
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-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH
show the reaction diagram
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ir
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
show the reaction diagram
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-
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?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
show the reaction diagram
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-
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?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
show the reaction diagram
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?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
187% activity compared to D-lactaldehyde
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?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
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?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
show the reaction diagram
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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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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
show the reaction diagram
A3LNE3, A3M013
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-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
show the reaction diagram
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glyceraldehyde
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substrate inhibition
glycolaldehyde
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substrate inhibition
iodoacetate
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lactaldehyde
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substrate inhibition
methylglyoxal
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substrate inhibition
Mn2+
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50% inhibition at 10 mM
N-ethylmaleimide
p-chloromercuribenzoate
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p-hydroxymercuribenzoate
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50% inhibition at 1.5 mM
Zn2+
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50% inhibition at 0.4 mM
additional information
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iodoacetamide, Mn2+, Mg2+, Co2+, no effect at 5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
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dithiothreitol
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slight activation
glutathione
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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+
0.302 - 5.6
D-Lactaldehyde
0.14
glycoaldehyde
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.38
glycolaldehyde
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0.15
L-Glyceraldehyde
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0.04 - 10
L-lactaldehyde
1
methylglyoxal
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0.007 - 3.5
NAD+
0.0078
NADP+
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mutant F180T
4.5
phenaylacetaldehyd
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
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0.24 - 0.284
propionaldehyde
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
acetaldehyde
Escherichia coli
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.9
benzaldehyde
Escherichia coli
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
2
D-Lactaldehyde
Methanocaldococcus jannaschii
Q58806
100 mM TES pH 7.5, 2.5 mM NAD+
18.3
glycoaldehyde
Escherichia coli
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
0.5
phenaylacetaldehyd
Escherichia coli
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100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+
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1.8 - 3
propionaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00048
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whole cell lysate
0.00051
0.355
purified recombinant enzyme, S-lactaldehyde, NADP+
0.6
100 mM TES pH 7.5, 2.5 mM NAD+
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
2.1
purified recombinant enzyme, R-lactaldehyde, NAD+
2.28
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purified recombinant enzyme, (R)-D-lactaldehyde, NAD+
3.64
purified recombinant enzyme, S-lactaldehyde, NAD+
4.28
purified recombinant enzyme, glycolaldehyde, NAD+
4.43
purified recombinant enzyme, (R)-lactaldehyde, NAD+
6.4
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strain 3
6.95
purified recombinant enzyme, (S)-lactaldehyde, NAD+
8.94
purified recombinant enzyme, glycolaldehyde, NAD+
11.5
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purified recombinant enzyme, glycolaldehyde, NAD+
17
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strain JA-102
17.2
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purified recombinant enzyme, (S)-lactaldehyde, NAD+
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5 - 11
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
17% activity at pH 7.0, almost 100% activity at pH 10.0
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 hide
LITERATURE
25
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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rapid decline in activity above 60C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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no activity in the bloodstream stage of the parasite
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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gel filtration, SDS-PAGE
50000
SDS-PAGE
55000
SDS-PAGE; SDS-PAGE
70000
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gel filtration
100000
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sucrose density gradient centrifugation
210000
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gel-filtration
220000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 55000, SDS-PAGE; 1 * 55000, SDS-PAGE
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; in complex with NADH and lactate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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4C, stable
288132
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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pH 6.5, 10 min, 50% loss of activity
80
86% activity after 80C for 10 min
90
45% activity after 90C for 10 min
100
25% activity after 100C for 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis in absence of EDTA and beta-mercaptoethanol: complete loss of activity
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purified enzyme is extremely unstable, reactivation with halide ions e.g. Cl-, I-, Br-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 100 mM H2NaPO4, pH 7.5, 100 mM NaCl,0.025% 2-mercaptoethanol, 50% glycerol, stable for 6 months
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-20C, 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
anion-exchange chromatography
by gel filtration; three chromatography steps
mutant F180T purified to homogeneity (more than 95% pure), on Ni2+ resin
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Ni-affinity chromatography
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nickel-chelating affinity column
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nickel-chelating affinity column; nickel-chelating affinity column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21 as His-tag fusion protein
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expression in Escherichia coli; heterologous expression with taxadiene synthase in Escherichia coli BL21(DE3)
overexpression in Escherichia coli cells as a His6-tagged enzyme
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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 hide
LITERATURE
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
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