Information on EC 1.2.1.67 - vanillin dehydrogenase

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The enzyme appears in viruses and cellular organisms

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
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Manually annotated by BRENDA team
strain AN103
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Manually annotated by BRENDA team
strain KT2440
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain SYK-6
UniProt
Manually annotated by BRENDA team
strain SYK-6
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
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
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
coniferylaldehyde + NAD+ + H2O
coniferic acid + 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
p-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
show the reaction diagram
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + H+
show the reaction diagram
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
show the reaction diagram
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
show the reaction diagram
activity toward syringaldehyde is less than 5% of that toward vanillin
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-
?
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
show the reaction diagram
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 + 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
additional information
?
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the enzyme is involved in catabolism of ferulic acid
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.004 - 0.007
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
0.072
purified recombinant protein, low activity due to loss of activity during purification, pH 7.1 and 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 10
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 60
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high activity across a wide range of temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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SDS-PAGE and Western blot
110000
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gel filtration
250000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
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
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
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
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
nutrition