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
-
-
-
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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
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
jojoba
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
the enzyme is not involved in the long-chain base metabolism
physiological function
additional information
the dimeric FALDH displays a an element in its C-terminal region, a gatekeeper helix, which extends over the adjacent subunit, controlling the access to the substrate cavity and helping orientate both substrate cavities towards the membrane surface for efficient substrate transit between membranes and catalytic site. The gatekeeper helix is important for directing the substrate specificity of FALDH towards long-chain fatty aldehydes. Cys241 is the catalytic cysteine in the human enzyme
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a long-chain aldehyde + NAD+ + H2O
a long-chain carboxylate + NADH + 2 H+
show the reaction diagram
-
-
-
?
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
hexadecanoate + NADH + 2 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
a long-chain aldehyde + NAD+ + H2O
a long-chain carboxylate + NADH + 2 H+
show the reaction diagram
P51648
-
-
-
?
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
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-
?
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
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0.03 mM causes 100% inhibition
Chloral hydrate
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25 mM causes 29% inhibition
Disulfiram
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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
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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
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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
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-
1.44
benzaldehyde
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-
0.006
cis,cis-9,12-octadecadienal
-
-
0.012
cis-9-hexadecenal
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-
0.011
cis-9-octadecenal
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-
0.8
crotonaldehyde
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-
0.0038 - 0.023
decanal
0.004
decyl aldehyde
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-
0.006
dihydrophytal
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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
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-
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
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-
2.18
decanal
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2.23
dodecanal
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0.93
farnesal
-
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0.95
hexadecanal
-
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1.28
NAD+
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1.52
Octadecanal
-
-
0.86
Tetradecanal
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00879
-
glucose-grown cell
0.0932
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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
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
additional information
the dimeric FALDH displays a an element in its C-terminal region, a gatekeeper helix, which extends over the adjacent subunit, controlling the access to the substrate cavity and helping orientate both substrate cavities towards the membrane surface for efficient substrate transit between membranes and catalytic site. Three-dimensional structure analysis and modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
enzyme ALDH3B2 is modified by prenylation at its C-terminus. The modification greatly influences its membrane localization and enzymatic activity towards hexadecanal; enzyme ALDH3B3 is modified by prenylation at its C-terminus. The modification greatly influences its membrane localization and enzymatic activity towards hexadecanal
palmitoylation
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the human class 3 aldehyde dehydrogenase ALDH3A1, PDB ID 3SZA as search model, and modelling
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
-
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration
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
-
gene ALDH3A2, recombinant expression of Strep-tagged enzyme in Escherichia coli, the enzyme lacks the predicted transmembrane alpha-helical region (residues 464-485) that is not included in the expression constructs, due to incompatibility with the protein production process
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
C241S
site-directed mutagenesis, inactive active-site mutant
D245N
-
NAD+ cosubstrate binding is occuring but catalytic reduction is diminished
E207Q
site-directed mutagenesis, inactive mutant
E331Q
site-directed mutagenesis, inactive mutant
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
N112A
site-directed mutagenesis, inactive mutant
Q445R
-
substitution in the recombinant protein
T184M
-
disruption of NAD+ binding/utilisation
T184R
-
disruption of NAD+ binding/utilisation
Y113F
site-directed mutagenesis, the mutant activity is unaltered compared to wild-type
Y410F
site-directed mutagenesis, the mutant shows normal Vmax/KM levels against octanal and dodecanal and a somewhat reduced but still considerable catalytic capacity for hexadecanal
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine