Information on EC 1.2.1.48 - long-chain-aldehyde dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.2.1.48
-
RECOMMENDED NAME
GeneOntology No.
long-chain-aldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + NAD+ + H2O = a long-chain carboxylate + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fatty acid degradation
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-
SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NAD+ oxidoreductase
The best substrate is dodecylaldehyde.
CAS REGISTRY NUMBER
COMMENTARY hide
59298-89-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M-1
-
-
Manually annotated by BRENDA team
strain M-1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
; strain B23
UniProt
Manually annotated by BRENDA team
; strain B23
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
jojoba
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme is not involved in the long-chain base metabolism
physiological function
-
the likely physiological function of ALDH3B1 is to oxidize lipid-derived aldehydes generated in the plasma membrane
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
arachidic aldehyde + NAD+ + H2O
arachidic acid + NADH
show the reaction diagram
-
-
-
?
behenic aldehyde + NAD+ + H2O
behenic acid + NADH
show the reaction diagram
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
?
cis,cis-9,12-octadecadienal + NAD+ + H2O
cis,cis-9,12-octadecadienoic acid + NADH
show the reaction diagram
cis-11-hexadecenal + NAD+ + H2O
cis-11-hexadecenoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
cis-9-hexadecenal + NAD+ + H2O
cis-9-hexadecenoic acid + NADH
show the reaction diagram
cis-9-octadecenal + NAD+ + H2O
cis-9-octadecenoic acid + NADH
show the reaction diagram
-
-
-
?
crotonaldehyde + NAD+ + H2O
crotonic acid + NADH
show the reaction diagram
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
show the reaction diagram
decanal + NAD+ + H2O
decanoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrophytal + NAD+ + H2O
(3R,S,7R,11R)-3,7,11,15-tetramethylhexadecanoic acid + NADH
show the reaction diagram
-
-
-
?
dodecanal + NAD+ + H2O
dodecanoic acid + NADH
show the reaction diagram
dodecanal + NAD+ + H2O
dodecanoic acid + NADH + H+
show the reaction diagram
farnesal + NAD+ + H2O
farnesoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
glutaraldehyde + NAD+
glutaric acid + NADH
show the reaction diagram
-
-
-
?
glyceraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
?
heptanal + NAD+ + H2O
heptanoic acid + NADH
show the reaction diagram
-
-
-
?
heptanal + NAD+ + H2O
heptanoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
hexadecanal + NAD+ + H2O
hexadecanoic acid + NADH
show the reaction diagram
hexadecanal + NAD+ + H2O
hexadecanoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
hexanal + NAD+ + H2O
?
show the reaction diagram
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
-
-
-
?
hexanal + NAD+ + H2O
hexanoic acid + NADH + H+
show the reaction diagram
50% of the activity with tetradecanal
-
-
?
long-chain aldehyde + NAD+
?
show the reaction diagram
long-chain aldehyde + NAD+ + H2O
long-chain acid anion + NADH
show the reaction diagram
long-chain aldehyde + NAD+ + H2O
long-chain carboxylate + NADH
show the reaction diagram
m-fluorobenzaldehyde + NAD+ + H2O
m-fluorobenzoic acid + NADH + H+
show the reaction diagram
-
-
-
?
m-methylbenzaldehyde + NAD+ + H2O
m-methylbenzoic acid + NADH
show the reaction diagram
-
36% activity toward tetradecanal
-
?
nonanal + NAD+ + H2O
nonanoic acid + NADH + H+
show the reaction diagram
-
-
-
?
o-fluorobenzaldehyde + NAD+ + H2O
o-fluorobenzoic acid + NADH + H+
show the reaction diagram
-
-
-
?
octadecanal + NAD+ + H2O
octadecanoic acid + NADH
show the reaction diagram
-
-
-
?
octadecanal + NAD+ + H2O
octadecanoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
octanal + NAD+ + H2O
octanoic acid + NADH + H+
show the reaction diagram
p-chlorobenzaldehyde + NAD+ + H2O
p-chlorobenzoic acid + NADH + H+
show the reaction diagram
-
-
-
?
p-cumic aldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
?
p-fluorobenzaldehyde + NAD+ + H2O
p-fluorobenzoic acid + NADH + H+
show the reaction diagram
-
-
-
?
pentadecanal + NAD+ + H2O
pentadecanoic acid + NADH
show the reaction diagram
-
-
-
?
phytenal + NAD+
phytenic acid + NADH
show the reaction diagram
propionaldehyde + NAD+ + H2O
propionic acid + NADH
show the reaction diagram
-
-
-
?
pyrenedecanal + NAD+ + H2O
pyrenedecanoic acid + NADH
show the reaction diagram
retinal + NAD+ + H2O
?
show the reaction diagram
-
-
-
?
tetradecanal + NAD+ + H2O
tetradecanoic acid + NADH
show the reaction diagram
tetradecanal + NAD+ + H2O
tetradecanoic acid + NADH + H+
show the reaction diagram
tetraeicosanal + NAD+ + H2O
tetraeicosanoic acid + NADH
show the reaction diagram
-
-
-
?
trans-2-decenal + NAD+ + H2O
trans-2-decenoic acid + NADH
show the reaction diagram
-
32% activity toward tetradecanal
-
?
trans-2-hexadecenal + NAD+ + H2O
trans-2-decenoic acid + NADH
show the reaction diagram
-
-
-
-
?
trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamic acid + NADH
show the reaction diagram
-
38% activity toward tetradecanal
-
?
additional information
?
-
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
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
?
show the reaction diagram
Q9FAB1
-
-
-
?
cis,cis-9,12-octadecadienal + NAD+ + H2O
cis,cis-9,12-octadecadienoic acid + NADH
show the reaction diagram
glyceraldehyde + NAD+ + H2O
?
show the reaction diagram
Q9FAB1
-
-
-
?
hexadecanal + NAD+ + H2O
hexadecanoic acid + NADH
show the reaction diagram
-
high activity
-
-
?
hexanal + NAD+ + H2O
?
show the reaction diagram
Q9FAB1
-
-
-
?
long-chain aldehyde + NAD+
?
show the reaction diagram
long-chain aldehyde + NAD+ + H2O
long-chain acid anion + NADH
show the reaction diagram
-
-
-
-
?
long-chain aldehyde + NAD+ + H2O
long-chain carboxylate + NADH
show the reaction diagram
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
p-cumic aldehyde + NAD+ + H2O
?
show the reaction diagram
Q9FAB1
-
-
-
?
phytenal + NAD+
phytenic acid + NADH
show the reaction diagram
-
the enzyme is involved in the breakdown of phytol
-
-
?
retinal + NAD+ + H2O
?
show the reaction diagram
Q9FAB1
-
-
-
?
trans-2-hexadecenal + NAD+ + H2O
trans-2-decenoic acid + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
about 50% of the activity with NADH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
2 mM, 2-3fold stimulation; activity is elevated 2fold in the presence of 2 mM
Ca2+
2 mM, 2-3fold stimulation; activity is elevated 2fold in the presence of 2 mM
Mg2+
-
1 mM causes 35% increase in activity
Mn2+
-
1 mM causes 24% increase in activity
Sr2+
2 mM, 2-3fold stimulation; activity is elevated 3fold in the presence of 2 mM
additional information
-
CaCl2, MgCl2, NaCl and KCl at concentration of 1 mM exert little effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
1 mM causes complete inhibition
alpha,p-dibromoacetophenone
-
0.03 mM causes 100% inhibition
Chloral hydrate
-
25 mM causes 29% inhibition
Disulfiram
-
0.065 mM causes 100% inhibition
EDTA
2 mM, 63% residual activity; 63% relative activity
Fe3+
-
1 mM causes complete inhibition
Hg2+
-
1 mM causes complete inhibition
iodoacetamide
-
10 mM causes 96% inhibition
iodoacetate
Mg2+
14% relative activity with 2 mM MgCl2 compared to the activity without metal ions; 2 mM, 14% residual activity
Mn2+
-
1 mM causes 37% inhibition
N-ethylmaleimide
p-chloromercuribenzoate
p-hydroxyacetophenone
-
0.25 mM causes 46% inhibition
Pb2+
-
1 mM causes complete inhibition
potassium cyanide
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1 mM causes 33% inhibition
Triton X-100
-
at a final concentration of 0.01%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alkane
transcriptional induction of Bt-aldh gene by alkane, Bt-aldh dramatically increases after 10 day cultivation, exactly when the alkane degradation starts
dithiothreitol
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5 mM causes 58% increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0343
(11Z)-hexadec-11-enal
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-
2.5
acetaldehyde
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-
0.038
arachidic aldehyde
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-
0.036
behenic aldehyde
-
-
1.44
benzaldehyde
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-
0.006
cis,cis-9,12-octadecadienal
-
-
0.012
cis-9-hexadecenal
-
-
0.011
cis-9-octadecenal
-
-
0.8
crotonaldehyde
-
-
0.0038 - 0.023
decanal
0.004
decyl aldehyde
-
-
0.006
dihydrophytal
-
-
0.0136 - 0.019
dodecanal
0.023
farnesal
-
-
1.7
Glutaraldehyde
-
-
0.0083 - 0.032
hexadecanal
0.05
Hexanal
-
-
0.18 - 0.28
NAD+
8.7
NADP+
-
reference substrate octadecanal
0.02 - 0.021
Octadecanal
0.032
octanal
-
-
0.028
Pentadecanal
-
-
1.3
propionaldehyde
-
-
0.0103 - 0.023
Tetradecanal
0.018
tetraeicosanal
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
(11Z)-hexadec-11-enal
Homo sapiens
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-
2.18
decanal
Homo sapiens
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2.23
dodecanal
Homo sapiens
-
-
0.93
farnesal
Homo sapiens
-
-
0.95
hexadecanal
Homo sapiens
-
-
1.28
NAD+
Homo sapiens
-
-
1.52
Octadecanal
Homo sapiens
-
-
0.86
Tetradecanal
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00879
-
glucose-grown cell
0.0932
-
stearyl alcohol-grown cell
0.098
-
alkane-grown cell
10.9
-
purified recombinant enzyme from Escherichia coli, tetradecanal used as substrate
33.3
-
-
additional information
110% relative activity with 2 mM MnCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 120% relative activity with 2 mM CoCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 14% relative activity with 2 mM MgCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 190% relative activity with 2 mM CaCl2 EDTA compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 210% relative activity with 2 mM BaCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 340% relative activity with 2 mM SrCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 63% relative activity with 2 mM EDTA compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 87% relative activity with 2 mM CuCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; 97% relative activity with 2 mM NiCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+; in the range of substrate aldehydes with carbon numbers C2 to C14, Bt-Aldh is the most active against C14, tetradecanal at 55°C, the activity against tetradecanal is 73times higher than that against octanal; relative activity is above 1% with 2 mM ZnCl2 compared to the activity without metal ions, pH 10, 50 mM glycine buffer, 37°C, 1 mM hexanal, 1 mM NAD+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.8
-
in glycine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
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pH 6.5: about 25% of activity maximum, pH 10: about 75% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 55
optimum condition for activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
; high activity
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
multilocational
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53886
8 * 53886, calculated, 8 * 55000, SDS-PAGE
53890
monomer is calculated from the 497 amino acid residues
54000
-
x * 54000, SDS-PAGE
55496
-
x * 55496, calculated from the deduced amino acid sequence
57000
-
x * 57000, SDS-PAGE
232000
-
gel filtration, purified recombinant enzyme from Escherichia coli
410000
estimated by gel filtration; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
octamer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
palmitoylation
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using the hanging drop vapor diffusion technique and iterative seeding techniques
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30 min, pH 7.5 to 9.0, more than 90% of activity remains
37
-
t1/2: 5 min, 100% loss of activity after 60 min
47
-
5 min, the purified enzyme retains only 13% of its original activity
52
-
5 min, 100% loss of activity
60
-
30 min, 90% of activity remains
70
30 min, 12.7% residual activity; activity decreases to 12.7% after a heat treatment at 70°C for 30 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM potassium phosphate, pH 7.5, 5% glycerol, 0.2 mM NAD+, 3 months, retains more than 80% of its original activity
-
4°C, 25 mM potassium phosphate, pH 7.5, 5% glycerol, 0.2 mM NAD+, 1 month, retains 67% of its original activity
-
frozen, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crude enzyme solution is applied to an anionic exchange column and eluted by linearly increasing the NaCl concentration from 0-1.0 M in 50 mM Tris-HCl at pH 7.0
including chromatography in a Resource Q column, recombinant enzyme from Escherichia coli also purified
-
recombinant His6-FADH purified by anion exchange and metal-chelate chromatography, to 90-95% purity
-
Strep-tag affinity chromatography and AMP-Sepharose column chromatography
-
using chromatography on columns consisting of omega-aminohexyl-agarose and 5'-AMP-Sepharose 4B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in FAA-K1A cells
-
expression and overproduction in Escherichia coli; expression in Escherichia coli
gene ald1 cloned from the chromosomal DNA of the bacterium and expressed in Escherichia coli
-
recombinant His6-FADH expressed in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression level is dramatically increased when alkane degradation is started
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D245N
-
NAD+ cosubstrate binding is occuring but catalytic reduction is diminished
G185A
-
disruption of NAD+ binding/utilisation
G412R
-
disruption of interaction of side-chains with substrate
H411Y
-
disruption of the key abstraction of the hydroxyl hydrogen
Q445R
-
substitution in the recombinant protein
T184M
-
disruption of NAD+ binding/utilisation
T184R
-
disruption of NAD+ binding/utilisation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine