Information on EC 1.2.1.67 - vanillin dehydrogenase

for references in articles please use BRENDA:EC1.2.1.67
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.2.1.67
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RECOMMENDED NAME
GeneOntology No.
vanillin dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
vanillin + NAD+ + H2O = vanillate + NADH + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vanillin and vanillate degradation I
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vanillin and vanillate degradation II
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Aminobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
vanillin:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
189767-93-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
Amycolatopsis sp. ATCC 39116 75iv2
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UniProt
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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UniProt
Manually annotated by BRENDA team
isolate P2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
DesV-like ALDHs form a distinct phylogenetic cluster separated from the vanillin dehydrogenase cluster, phylogenetic analyis; DesV-like ALDHs form a distinct phylogenetic cluster separated from the vanillin dehydrogenase cluster, phylogenetic analyis
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + 2 H+
show the reaction diagram
3-ethoxy-4-hydroxybenzaldehyde + NAD+ + H2O
3-ethoxy-4-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
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-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + 2 H+
show the reaction diagram
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-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
show the reaction diagram
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
show the reaction diagram
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
show the reaction diagram
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + 2 H+
show the reaction diagram
coniferyl aldehyde + NAD+ + H2O
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + NADH + H+
show the reaction diagram
coniferyl aldehyde + NAD+ + H2O
ferulic acid + NADH + 2 H+
show the reaction diagram
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-
-
?
coniferylaldehyde + NAD+ + H2O
coniferic acid + NADH + 2 H+
show the reaction diagram
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-
-
?
cyclohexanecarboxyaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
show the reaction diagram
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
show the reaction diagram
m-anisaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
show the reaction diagram
m-anisaldehyde + NAD+ + H2O
m-anisate + NADH + 2 H+
show the reaction diagram
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-
-
?
o-phthaldialdehyde + NAD+ + H2O
? + NADH + 2 H+
show the reaction diagram
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-
-
?
p-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
show the reaction diagram
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + 2 H+
show the reaction diagram
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-
-
?
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + H+
show the reaction diagram
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
show the reaction diagram
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
show the reaction diagram
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
show the reaction diagram
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
show the reaction diagram
syringaldehyde + NADP+ + H2O
syringate + NADPH + H+
show the reaction diagram
high activity
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-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
show the reaction diagram
vanillin + NAD+ + H2O
vanillate + NADH + H+
show the reaction diagram
best substrate
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-
?
vanillin + NADP+ + H2O
vanillate + NADPH + 2 H+
show the reaction diagram
veratraldehyde + NAD+ + H2O
veratrate + NADH + 2 H+
show the reaction diagram
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?
veratraldehyde + NAD+ + H2O
veratrate + NADH + H+
show the reaction diagram
activity toward veratraldehyde is less than 5% of that toward vanillin
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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
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
show the reaction diagram
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
show the reaction diagram
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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40% inhibition by 1 mM and 45% inhibition at 5 mM
Mg2+
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1.9fold increased enzyme activity with 1 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00048 - 0.412
syringaldehyde
0.00034 - 0.007
Vanillin
additional information
additional information
the enzyme shows positive cooperativity and substrate inhibition with some substrates. With benzaldehyde activity is observed, but the kinetic data cannot be fitted to Michaelis-Menten, cooperative or substrate inhibition kinetic models
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 0.99
syringaldehyde
0.79 - 3.03
Vanillin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 1700
syringaldehyde
2100 - 8800
Vanillin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.025
crude extract, when cells are previously cultivated with vanillin as the carbon source, pH 7.1 and 30C
0.05
substrate coniferyl aldehyde, purified recombinant enzyme, pH 7.0, 30C
0.072
purified recombinant protein, low activity due to loss of activity during purification, pH 7.1 and 30C
0.13
substrate veratraldehyde, purified recombinant enzyme, pH 7.0, 30C
0.36
substrate syringaldehyde, purified recombinant enzyme, pH 7.0, 30C
0.65
substrate m-anisaldehyde, purified recombinant enzyme, pH 7.0, 30C
0.98
substrate 4-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30C
1.04
substrate salicylaldehyde, purified recombinant enzyme, pH 7.0, 30C
1.24
substrate protocatechualdehyde, purified recombinant enzyme, pH 7.0, 30C
1.26
substrate benzaldehyde, purified recombinant enzyme, pH 7.0, 30C
1.38
substrate veratraldehyde, purified recombinant enzyme, pH 7.0, 30C
1.57
substrate vanillin, purified recombinant enzyme, pH 7.0, 30C
1.64
substrate benzaldehyde, purified recombinant enzyme, pH 7.0, 30C
1.68
substrate protocatechualdehyde, purified recombinant enzyme, pH 7.0, 30C
1.8
substrate syringaldehyde, purified recombinant enzyme, pH 7.0, 30C; substrate vanillin, purified recombinant enzyme, pH 7.0, 30C
1.9
substrate 4-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30C
2.09
substrate 3-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30C
2.12
substrate coniferyl aldehyde, purified recombinant enzyme, pH 7.0, 30C; substrate salicylaldehyde, purified recombinant enzyme, pH 7.0, 30C
2.22
substrate m-anisaldehyde, purified recombinant enzyme, pH 7.0, 30C
4.39
substrate 3-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30C
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9.5
activity range, profile overview
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 60
activity range, profile overview
35 - 60
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high activity across a wide range of temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49500
monomer, gel filtration
50301
x * 50301, SDS-PAGE
55000
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SDS-PAGE and Western blot
92300
dimer, gel filtration
110000
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gel filtration
120000
recombinant enzyme, gel filtration and native PAGE
159000
trimer, gel filtration
199200
tetramer, gel filtration
210000
crosslinking and gel filtration
220000
recombinant enzyme, gel filtration and native PAGE
250000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 55173, recombinant enzyme, SDS-PAGE
homodimer
homotetramer
oligomer
tetramer
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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30-min incubation at 30C
725035
7 - 8
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30 min incubation at 30C
725035
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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stable up to 30 min
35
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stable up to 30 min
85
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inactivation
additional information
the redox cofactor NADP+ and substrates increase the thermal stability of the protein, thermal stabilities (Tm) of Cd36_03230p in the presence of various potential substrates, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after storage at 4C for 24 h, the enzyme exhibits 86% of its former activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by DEAE-Sepharose FF column, butyl-Sepharose column and Resource Q column chromatography
partially purified by (NH4)2SO4 precipitation but it losts activity during attempted chromatographic steps
purified to apparent electrophoretic homogeneity using His SpinTrap columns
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pET-28a expression vector and transformed into Escherichia coli
cosmid library of SYK-6 strain transferred to Sphingomonas paucimobilis IAM12578. LigV expressed in Escherichia coli BL21(DE3)
expression in Escherichia coli
gene CD36-03230, recombinant expression in Escherichia coli
gene desV or SLG_28320, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of desV disruption mutants; gene ligV or SLG_07060, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli BL21(DE3)
gene vdh, phylogenetic tree
gene yfmT, DNA and amino acid sequence determination and analysis, recombinant overexpression of C-terminally HIs6-tagged enzyme in Escherchia coli strain JM109/pNG533.1
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vdh gene cloned into pET23a(+)vector heterologously expressed with C-terminal His6-tag in Escherichia coli BL21(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C292A
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
E199A
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+ the activity of E199A decreases to 78% of the wild-type activity
E258A
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme
K180A
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
N157A
site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
C292A
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site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
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E199A
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site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+ the activity of E199A decreases to 78% of the wild-type activity
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K180A
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site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
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N157A
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site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
Amycolatopsis sp. ATCC 39116 vdh mutant represents an optimized and industrially applicable platform for biotechnological production of natural vanillin
nutrition
synthesis
Show AA Sequence (113 entries)
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