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3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + 2 H+
3-ethoxy-4-hydroxybenzaldehyde + NAD+ + H2O
3-ethoxy-4-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
5-hydroxymethylfurfural + NAD+ + H2O
5-hydroxymethyl-2-furancarboxylic acid + NADH + 2 H+
anisaldehyde + NAD+ + H2O
anisoate + NADH + 2 H+
-
15% activity compared to vanillin
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + 2 H+
coniferyl aldehyde + NAD+ + H2O
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + NADH + H+
coniferyl aldehyde + NAD+ + H2O
ferulic acid + NADH + 2 H+
-
-
-
?
coniferylaldehyde + NAD+ + H2O
coniferic acid + NADH + 2 H+
-
-
-
?
cyclohexanecarboxyaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
isovanillin + NAD+ + H2O
isovanillate + NADH + 2 H+
-
49% activity compared to vanillin
-
-
?
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
m-anisaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
m-anisaldehyde + NAD+ + H2O
m-anisate + NADH + 2 H+
-
-
-
?
o-phthaldialdehyde + NAD+ + H2O
? + NADH + 2 H+
-
-
-
?
p-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + 2 H+
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + H+
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
syringaldehyde + NADP+ + H2O
syringate + NADPH + H+
high activity
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
vanillin + NAD+ + H2O
vanillate + NADH + H+
best substrate
-
-
?
vanillin + NADP+ + H2O
vanillate + NADPH + 2 H+
veratraldehyde + NAD+ + H2O
veratrate + NADH + H+
additional information
?
-
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + 2 H+
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
no reduction of vanillic acid to vanillin in crude cell extract observed, metabolism of ferulic acid to vanillic acid
-
ir
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
no reduction of vanillic acid to vanillin in crude cell extract observed, metabolism of ferulic acid to vanillic acid
-
ir
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
r
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
r
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
r
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
r
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
r
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
56% activity compared to vanillin
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
-
70% relative activity compared to vanillin
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
-
70% relative activity compared to vanillin
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
-
77% relative activity compared to vanillin
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + 2 H+
-
77% relative activity compared to vanillin
-
-
?
5-hydroxymethylfurfural + NAD+ + H2O
5-hydroxymethyl-2-furancarboxylic acid + NADH + 2 H+
-
the tolerance of the recombinant enzyme toward 5-hydroxymethylfurfural is up to 200 mM
-
-
?
5-hydroxymethylfurfural + NAD+ + H2O
5-hydroxymethyl-2-furancarboxylic acid + NADH + 2 H+
-
the tolerance of the recombinant enzyme toward 5-hydroxymethylfurfural is up to 200 mM
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
66% activity in comparison to vanillin
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
79% activity compared to vanillin
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + 2 H+
-
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + 2 H+
-
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + 2 H+
-
-
-
?
coniferyl aldehyde + NAD+ + H2O
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + NADH + H+
activity toward coniferyl aldehyde is less than 5% of that toward vanillin
-
-
?
coniferyl aldehyde + NAD+ + H2O
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + NADH + H+
activity toward coniferyl aldehyde is less than 5% of that toward vanillin
-
-
?
cyclohexanecarboxyaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
cyclohexanecarboxyaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
-
-
?
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
-
48% relative activity compared to vanillin
-
-
?
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
-
48% relative activity compared to vanillin
-
-
?
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
-
285% relative activity compared to vanillin
-
-
?
isovanillin + NADP+ + H2O
isovanillate + NADPH + 2 H+
-
285% relative activity compared to vanillin
-
-
?
m-anisaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
-
-
?
m-anisaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
-
-
?
p-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
-
-
?
p-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
-
-
?
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + 2 H+
-
-
-
?
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + 2 H+
-
91% activity compared to vanillin
-
-
?
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + H+
-
-
-
?
protocatechualdehyde + NAD+ + H2O
protocatechuate + NADH + H+
-
-
-
?
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
-
94% relative activity compared to vanillin
-
-
?
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
-
94% relative activity compared to vanillin
-
-
?
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
-
146% relative activity compared to vanillin
-
-
?
protocatechualdehyde + NADP+ + H2O
protocatechuate + NADPH + 2 H+
-
146% relative activity compared to vanillin
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
48% activity compared to vanillin
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
-
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
-
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
very low activity
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
high activity
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
from syringyl lignin degradation of hardwood
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
very low activity, from syringyl lignin degradation of hardwood
-
-
?
syringaldehyde + NAD+ + H2O
syringate + NADH + H+
activity toward syringaldehyde is less than 5% of that toward vanillin
-
-
?
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
-
29% relative activity compared to vanillin
-
-
?
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
-
29% relative activity compared to vanillin
-
-
?
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
-
23% relative activity compared to vanillin
-
-
?
syringaldehyde + NADP+ + H2O
syringate + NADPH + 2 H+
-
23% relative activity compared to vanillin
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
no enzyme activity observed in the absence of NAD+, no oxidation of vanillin detectable when NADP+ used as cofactor
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
higher activity with NAD+ than with NADP+, relative activity with NADP1 is approximately 10%
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
higher activity with NAD+ than with NADP+, relative activity with NADP1 is approximately 10%
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
vdh mutant Rhodococcus jostii RHA045 is unable to grow on 1 mM vanillin as the sole organic substrate but grows on 1 mM vanillate with kinetics similar to that of RHA1, mutant rescue by vdh harbouring pTipvdh plasmid
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
best substrate
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
from guaiacol lignin degradation of softwood
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
-
-
-
?
vanillin + NAD+ + H2O
vanillate + NADH + 2 H+
-
100% activity
-
-
?
vanillin + NADP+ + H2O
vanillate + NADPH + 2 H+
-
no activity with NAD+, strain TA1 exhibits oxidation activity specifically under alkaline conditions
-
-
?
vanillin + NADP+ + H2O
vanillate + NADPH + 2 H+
-
no activity with NAD+, strain TA1 exhibits oxidation activity specifically under alkaline conditions
-
-
?
veratraldehyde + NAD+ + H2O
veratrate + NADH + H+
-
-
-
?
veratraldehyde + NAD+ + H2O
veratrate + NADH + H+
activity toward veratraldehyde is less than 5% of that toward vanillin
-
-
?
veratraldehyde + NAD+ + H2O
veratrate + NADH + H+
-
12% activity compared to vanillin
-
-
?
additional information
?
-
vdh deletion mutant loses its ability to grow on vanillin and does not show vanillin dehydrogenase activity, 2.3fold higher vanillin concentration in vdh mutants observed when ferulic acid is provided for biotransformation in a cultivation experiment
-
-
?
additional information
?
-
-
vdh deletion mutant loses its ability to grow on vanillin and does not show vanillin dehydrogenase activity, 2.3fold higher vanillin concentration in vdh mutants observed when ferulic acid is provided for biotransformation in a cultivation experiment
-
-
?
additional information
?
-
-
4-hydroxy-3-methoxycinnamaldehyde and cinnamaldehyde are poor substrates
-
-
?
additional information
?
-
-
4-hydroxy-3-methoxycinnamaldehyde and cinnamaldehyde are poor substrates
-
-
?
additional information
?
-
the enzyme has no detectable activity with vanillin suggesting that the annotation is incorrect. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile156) at key position in the active site, instead of e.g. Met, further strengthening this hypothesis
-
-
?
additional information
?
-
the enzyme has no detectable activity with vanillin suggesting that the annotation is incorrect. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile156) at key position in the active site, instead of e.g. Met, further strengthening this hypothesis
-
-
?
additional information
?
-
product dentification by mass spectroscopic analysis
-
-
?
additional information
?
-
-
product dentification by mass spectroscopic analysis
-
-
?
additional information
?
-
product dentification by mass spectroscopic analysis
-
-
?
additional information
?
-
-
the enzyme is involved in catabolism of ferulic acid
-
-
?
additional information
?
-
-
the enzyme is involved in catabolism of ferulic acid
-
-
?
additional information
?
-
enzyme DesV shows a broad range of activity against benzaldehyde derivatives, substrate specificity, overview
-
-
?
additional information
?
-
enzyme DesV shows a broad range of activity against benzaldehyde derivatives, substrate specificity, overview
-
-
?
additional information
?
-
enzyme LigV shows a broad range of activity against benzaldehyde derivatives, substrate specificity, overview
-
-
?
additional information
?
-
enzyme LigV shows a broad range of activity against benzaldehyde derivatives, substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with NADP+ or syringaldehyde
-
-
-
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Aortic Valve Stenosis
Cell Sources for Tissue Engineering Strategies to Treat Calcific Valve Disease.
Brain Injuries, Traumatic
A review of the neuroprotective role of vitamin D in traumatic brain injury with implications for supplementation post-concussion.
Brain Injuries, Traumatic
Progesterone and vitamin d hormone as a biologic treatment of traumatic brain injury in the aged.
Carcinoma, Ovarian Epithelial
Missing information in statewide and national cancer databases: Correlation with health risk factors, geographic disparities, and outcomes.
Congenital Abnormalities
Evolution of an integrated public health surveillance system.
COVID-19
Assessment of Day-7 Postexposure Testing of Asymptomatic Contacts of COVID-19 Patients to Evaluate Early Release from Quarantine - Vermont, May-November 2020.
Friedreich Ataxia
Effect of a valine load test on plasma alpha-keto acids in Friedreich ataxia.
Infections
Post-ischemic stroke systemic inflammation: Immunomodulation by progesterone and vitamin D hormone.
Ischemic Stroke
Vitamin D deficiency increases blood-brain barrier dysfunction after ischemic stroke in male rats.
Neoplasms
Missing information in statewide and national cancer databases: Correlation with health risk factors, geographic disparities, and outcomes.
Salmonella Infections
Salmonellosis Outbreak After a Large-Scale Food Event in Virginia, 2017.
Sarcoma 180
Lentinan augments skin reaction induced by bradykinin: its correlation with vascular dilatation and hemorrhage responses and antitumor activities.
Stroke
Combination treatment with progesterone and vitamin D hormone is more effective than monotherapy in ischemic stroke: The role of BDNF/TrkB/Erk1/2 signaling in neuroprotection.
Stroke
Post-ischemic stroke systemic inflammation: Immunomodulation by progesterone and vitamin D hormone.
Stroke
Vitamin D deficiency increases blood-brain barrier dysfunction after ischemic stroke in male rats.
Stroke
Vitamin D hormone confers neuroprotection in parallel with downregulation of L-type calcium channel expression in hippocampal neurons.
Trichomonas Infections
[Comparing the Occurrence of Trichomonas vaginalis Infections Today to Ten Years Ago Among Women Prostitutes and Gynecology and Obstetrics Patients].
Vaginal Discharge
[Comparing the Occurrence of Trichomonas vaginalis Infections Today to Ten Years Ago Among Women Prostitutes and Gynecology and Obstetrics Patients].
vanillin dehydrogenase deficiency
A review of the neuroprotective role of vitamin D in traumatic brain injury with implications for supplementation post-concussion.
vanillin dehydrogenase deficiency
Effect of a valine load test on plasma alpha-keto acids in Friedreich ataxia.
vanillin dehydrogenase deficiency
Progesterone and vitamin d hormone as a biologic treatment of traumatic brain injury in the aged.
vanillin dehydrogenase deficiency
Progesterone and vitamin D: Improvement after traumatic brain injury in middle-aged rats.
vanillin dehydrogenase deficiency
Vitamin D deficiency increases blood-brain barrier dysfunction after ischemic stroke in male rats.
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0.025
crude extract, when cells are previously cultivated with vanillin as the carbon source, pH 7.1 and 30°C
0.05
substrate coniferyl aldehyde, purified recombinant enzyme, pH 7.0, 30°C
0.072
purified recombinant protein, low activity due to loss of activity during purification, pH 7.1 and 30°C
0.13
substrate veratraldehyde, purified recombinant enzyme, pH 7.0, 30°C
0.36
substrate syringaldehyde, purified recombinant enzyme, pH 7.0, 30°C
0.65
substrate m-anisaldehyde, purified recombinant enzyme, pH 7.0, 30°C
0.98
substrate 4-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.04
substrate salicylaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.24
substrate protocatechualdehyde, purified recombinant enzyme, pH 7.0, 30°C
1.26
substrate benzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.38
substrate veratraldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.57
substrate vanillin, purified recombinant enzyme, pH 7.0, 30°C
1.64
substrate benzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.68
substrate protocatechualdehyde, purified recombinant enzyme, pH 7.0, 30°C
1.9
substrate 4-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
2.09
substrate 3-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
2.22
substrate m-anisaldehyde, purified recombinant enzyme, pH 7.0, 30°C
4.39
substrate 3-hydroxybenzaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.8
substrate syringaldehyde, purified recombinant enzyme, pH 7.0, 30°C
1.8
substrate vanillin, purified recombinant enzyme, pH 7.0, 30°C
2.12
substrate coniferyl aldehyde, purified recombinant enzyme, pH 7.0, 30°C
2.12
substrate salicylaldehyde, purified recombinant enzyme, pH 7.0, 30°C
additional information
no VDH activity detectable in cells that are cultivated with gluconate as the sole carbon source
additional information
-
no VDH activity detectable in cells that are cultivated with gluconate as the sole carbon source
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evolution
DesV-like ALDHs form a distinct phylogenetic cluster separated from the vanillin dehydrogenase cluster, phylogenetic analyis
malfunction
a gene vdh deletion mutant of Amycolatopsis sp. strain ATCC 39116 shows increased levels of accumulated vanillin
malfunction
disruption of desV in SYK-6 results in a significant reduction in growth on syringaldehyde and in syringaldehyde oxidation activity. A desV-ligV double mutant almost completely loses its ability to grow on syringaldehyde. Purified DesV shows similar kcat/Km values for syringaldehyde and vanillin, whereas LigV substantially prefers vanillin over syringaldehyde
malfunction
the vdh deletion mutant partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde
malfunction
-
a gene vdh deletion mutant of Amycolatopsis sp. strain ATCC 39116 shows increased levels of accumulated vanillin
-
malfunction
-
the vdh deletion mutant partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde
-
metabolism
Amycolatopsis sp. ATCC 39116 is capable of synthesizing large amounts of vanillin from the natural substrate ferulic acid
metabolism
enzyme is involved in lignin degradation because one degradation product of lignin is vanillin
metabolism
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in strain 3NA, ferulic acid is converted to a substance identified as 4-vinylguaiacol (2-methoxy-4-vinylphenol), and vanillin is converted to ca. 97% guaiacol and 3 % vanillyl alcohol, whereas vanillic acid is completely converted to guaiacol. Vanillin is converted to guaiacol, forming vanillic acid as an intermediate product
metabolism
-
in strain 3NA, ferulic acid is converted to a substance identified as 4-vinylguaiacol (2-methoxy-4-vinylphenol), and vanillin is converted to ca. 97% guaiacol and 3 % vanillyl alcohol, whereas vanillic acid is completely converted to guaiacol. Vanillin is converted to guaiacol, forming vanillic acid as an intermediate product
-
physiological function
enzyme DesV plays a major role in syringaldehyde catabolism
physiological function
vanillin dehydrogenase is a crucial enzyme involved in the degradation of lignin-derived phenylpropanoids, such as vanillin, vanillate, caffeate, p-coumarate, and cinnamate
physiological function
-
vanillin dehydrogenase is a crucial enzyme involved in the degradation of lignin-derived phenylpropanoids, such as vanillin, vanillate, caffeate, p-coumarate, and cinnamate
-
additional information
enzyme molecular modeling, dimeric model construction using the structure of ALDH domains of Geobacter sulfurreducens PutA, PDB ID 4NMB, for the enzyme dimer and sheep liver class 1 aldehyde dehydrogenase structure, 1BXS, as the template fo rthe tetramer. molecularmodelling of Cd36_03230p predicts that it has a similar fold to other aldehyde dehydrogenases
additional information
residues E258 and C292 are identified as the candidate conserved catalytic residues whereas N157, K180 and E199 are identified as the candidate cofactor interactive sites in VDHATCC13032, all residues are important for enzyme activity
additional information
-
residues E258 and C292 are identified as the candidate conserved catalytic residues whereas N157, K180 and E199 are identified as the candidate cofactor interactive sites in VDHATCC13032, all residues are important for enzyme activity
additional information
-
residues E258 and C292 are identified as the candidate conserved catalytic residues whereas N157, K180 and E199 are identified as the candidate cofactor interactive sites in VDHATCC13032, all residues are important for enzyme activity
-
additional information
-
enzyme molecular modeling, dimeric model construction using the structure of ALDH domains of Geobacter sulfurreducens PutA, PDB ID 4NMB, for the enzyme dimer and sheep liver class 1 aldehyde dehydrogenase structure, 1BXS, as the template fo rthe tetramer. molecularmodelling of Cd36_03230p predicts that it has a similar fold to other aldehyde dehydrogenases
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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
-
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
-
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
-
additional information
metabolic engineering of the actinomycete Amycolatopsis sp. strain ATCC 39116 towards enhanced production of natural vanillin. Degradation of vanillin is decreased by more than 90% through deletion of the vdh gene, which codes for the central vanillin catabolism enzyme, vanillin dehydrogenase. This mutation results in improvement of the final concentration of vanillin by more than 2.2 g/liter, with a molar yield of 80.9%. Further improvement is achieved with constitutive expression of the vanillin anabolism genes ech and fcs, coding for the enzymes feruloyl-coenzyme A (CoA) synthetase (fcs) and enoyl-CoA hydratase/aldolase (ech). The transcription of both genes is shown to be induced by ferulic acid, which explains the unwanted adaptation phase in the fermentation process before vanillin is efficiently produced by the wild-type cells. Through the constitutive and enhanced expression of the two genes, the adaptation phase is eliminated and a final vanillin concentration of 19.3 g/liter, with a molar yield of 94.9%, is obtained. Moreover, an even higher final vanillin concentration of 22.3 g/liter is achieved, at the expense of a lower molar yield, by using an improved feeding strategy. The vanillin is produced almost without by-products, with a molar yield that nearly approaches the theoretical maximum. Generation of a vdh deletion mutant with replacement of vdh gene by kanamycin resistance gene, deletion of vdh via homologous recombination
additional information
-
metabolic engineering of the actinomycete Amycolatopsis sp. strain ATCC 39116 towards enhanced production of natural vanillin. Degradation of vanillin is decreased by more than 90% through deletion of the vdh gene, which codes for the central vanillin catabolism enzyme, vanillin dehydrogenase. This mutation results in improvement of the final concentration of vanillin by more than 2.2 g/liter, with a molar yield of 80.9%. Further improvement is achieved with constitutive expression of the vanillin anabolism genes ech and fcs, coding for the enzymes feruloyl-coenzyme A (CoA) synthetase (fcs) and enoyl-CoA hydratase/aldolase (ech). The transcription of both genes is shown to be induced by ferulic acid, which explains the unwanted adaptation phase in the fermentation process before vanillin is efficiently produced by the wild-type cells. Through the constitutive and enhanced expression of the two genes, the adaptation phase is eliminated and a final vanillin concentration of 19.3 g/liter, with a molar yield of 94.9%, is obtained. Moreover, an even higher final vanillin concentration of 22.3 g/liter is achieved, at the expense of a lower molar yield, by using an improved feeding strategy. The vanillin is produced almost without by-products, with a molar yield that nearly approaches the theoretical maximum. Generation of a vdh deletion mutant with replacement of vdh gene by kanamycin resistance gene, deletion of vdh via homologous recombination
-
additional information
generation of a vdh deletion mutant, which partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde
additional information
-
generation of a vdh deletion mutant, which partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde
additional information
-
generation of a vdh deletion mutant, which partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde
-
additional information
-
insertional mutagenesis of the vanillin dehydrogenase gene renders the strain unable to grow on vanillin or ferulic acid
additional information
-
insertional mutagenesis of the vanillin dehydrogenase gene renders the strain unable to grow on vanillin or ferulic acid
-
additional information
generation of desV disruption mutants
additional information
generation of desV disruption mutants
additional information
insertional inactivation of ligV negatively affects growth on vanillin (only 11% of the vanillin dehydrogenase activity of the wild-type strain), whereas growth on syringaldehyde, veratraldehyde and coniferyl aldehyde is almost the same as the wild-type activity. Dehydrogenase activity towards benzaldehyde, p-hydroxybenzaldehyde, protocatechualdehyde and m-anisaldehyde is decreased to 27%, 35%, 14% and 54%, respectively of the wild-type activity. Mutant retains ability to grow on ferulate
additional information
-
insertional inactivation of ligV negatively affects growth on vanillin (only 11% of the vanillin dehydrogenase activity of the wild-type strain), whereas growth on syringaldehyde, veratraldehyde and coniferyl aldehyde is almost the same as the wild-type activity. Dehydrogenase activity towards benzaldehyde, p-hydroxybenzaldehyde, protocatechualdehyde and m-anisaldehyde is decreased to 27%, 35%, 14% and 54%, respectively of the wild-type activity. Mutant retains ability to grow on ferulate
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Overhage, J.; Priefert, H.; Rabenhorst, J.; Steinbuchel, A.
Biotransformation of eugenol to vanillin by a mutant of Pseudomonas sp. strain HR199 constructed by disruption of the vanillin dehydrogenase (vdh) gene
Appl. Microbiol. Biotechnol.
52
820-828
1999
Pseudomonas sp.
brenda
Narbad, A.; Gasson, M.J.
Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly isolated strain of Pseudomonas fluorescens
Microbiology
144
1397-1405
1998
Pseudomonas fluorescens
brenda
Priefert, H.; Rabenhorst, J.; Steinbuchel, A.
Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate
J. Bacteriol.
179
2595-2607
1997
Pseudomonas sp.
brenda
Perestelo, F.; Falcon, M.A.; De La Fuente, G.
Production of vanillic acid from vanillin by resting cells of Serratia marcescens
Appl. Environ. Microbiol.
55
1660-1662
1989
Serratia marcescens
brenda
Pometto, A.L.; Crawford, D.L.
Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus
Appl. Environ. Microbiol.
45
1582-1585
1983
Streptomyces viridosporus
brenda
Plaggenborg, R.; Overhage, J.; Steinbuchel, A.; Priefert, H.
Functional analyses of genes involved in the metabolism of ferulic acid in Pseudomonas putida KT2440
Appl. Microbiol. Biotechnol.
61
528-535
2003
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Martinez-Cuesta, M.d.; Payne, J.; Hanniffy, S.B.; Gasson, M.J.; Narbad, A.
Functional analysis of the vanillin pathway in a vdh-negative mutant strain of Pseudomonas fluorescens AN103
Enzyme Microb. Technol.
37
131-138
2005
Pseudomonas fluorescens, Pseudomonas fluorescens AN103
-
brenda
Masai, E.; Yamamoto, Y.; Inoue, T.; Takamura, K.; Hara, H.; Kasai, D.; Katayama, Y.; Fukuda, M.
Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6
Biosci. Biotechnol. Biochem.
71
2487-2492
2007
Sphingomonas paucimobilis (A2PZP3), Sphingomonas paucimobilis SYK-6 (A2PZP3), Sphingomonas paucimobilis SYK-6
brenda
Chen, H.P.; Chow, M.; Liu, C.C.; Lau, A.; Liu, J.; Eltis, L.D.
Vanillin catabolism in Rhodococcus jostii RHA1
Appl. Environ. Microbiol.
78
586-588
2012
Rhodococcus jostii (Q0SCE7)
brenda
Fleige, C.; Hansen, G.; Kroll, J.; Steinbuechel, A.
Investigation of the Amycolatopsis sp. strain ATCC 39116 vanillin dehydrogenase and its impact on the biotechnical production of vanillin
Appl. Environ. Microbiol.
79
81-90
2013
Amycolatopsis sp. (K9UV87), Amycolatopsis sp.
brenda
Mitsui, R.; Hirota, M.; Tsuno, T.; Tanaka, M.
Purification and characterization of vanillin dehydrogenases from alkaliphile Micrococcus sp. TA1 and neutrophile Burkholderia cepacia TM1
FEMS Microbiol. Lett.
303
41-47
2010
Burkholderia cepacia, Micrococcus sp., Micrococcus sp. TA1, Burkholderia cepacia TM1
brenda
Fleige, C.; Meyer, F.; Steinbuechel, A.
Metabolic engineering of the actinomycete Amycolatopsis sp. strain ATCC 39116 towards enhanced production of natural vanillin
Appl. Environ. Microbiol.
82
3410-3419
2016
Amycolatopsis sp. ATCC 39116 (K9UV87), Amycolatopsis sp. ATCC 39116 75iv2 (K9UV87)
brenda
Graf, N.; Wenzel, M.; Altenbuchner, J.
Identification and characterization of the vanillin dehydrogenase YfmT in Bacillus subtilis 3NA
Appl. Microbiol. Biotechnol.
100
3511-3521
2016
Bacillus subtilis, Bacillus subtilis 3NA
brenda
Kaur, B.; Chakraborty, D.; Kumar, B.
Phenolic biotransformations during conversion of ferulic acid to vanillin by lactic acid bacteria
BioMed Res. Int.
2013
590359
2013
Streptomyces avermitilis
brenda
Chakraborty, D.; Kaur, B.; Obulisamy, K.; Selvam, A.; Wong, J.W.
Agrowaste to vanillin conversion by a natural Pediococcus acidilactici strain BD16
Environ. Technol.
38
1823-1834
2016
Pediococcus acidilactici, Pediococcus acidilactici BD16
brenda
Datta, S.; Annapure, U.; Timson, D.
Characterization of Cd36-03230p, a putative vanillin dehydrogenase from Candida dubliniensis
RSC Adv.
6
99774-99780
2016
Candida dubliniensis (B9W7C4), Candida dubliniensis CD36 (B9W7C4)
-
brenda
Ding, W.; Si, M.; Zhang, W.; Zhang, Y.; Chen, C.; Zhang, L.; Lu, Z.; Chen, S.; Shen, X.
Functional characterization of a vanillin dehydrogenase in Corynebacterium glutamicum
Sci. Rep.
5
8044
2015
Corynebacterium glutamicum (Q8NMB0), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q8NMB0)
brenda
Kamimura, N.; Goto, T.; Takahashi, K.; Kasai, D.; Otsuka, Y.; Nakamura, M.; Katayama, Y.; Fukuda, M.; Masai, E.
A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde
Sci. Rep.
7
44422
2017
Sphingobium sp. SYK-6 (G2IKV5), Sphingobium sp. SYK-6 (G2IMC6)
brenda
Nishimura, M.; Kawakami, S.; Otsuka, H.
Molecular cloning and characterization of vanillin dehydrogenase from Streptomyces sp. NL15-2K
BMC Microbiol.
18
154
2018
Streptomyces sp. NL15-2K
brenda
Zhang, X.Y.; Ou, X.Y.; Fu, Y.J.; Zong, M.H.; Li, N.
Efficient synthesis of 5-hydroxymethyl-2-furancarboxylic acid by Escherichia coli overexpressing aldehyde dehydrogenases
J. Biotechnol.
307
125-130
2020
Comamonas testosteroni, Comamonas testosteroni SC1588
brenda