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(R)-1-(4'-Hydroxyphenyl)ethanol + O2
?
-
-
-
-
?
(R,S)-1-(4'-Hydroxyphenyl)propanol + O2
?
-
-
-
-
?
(S)-1-(4'-Hydroxyphenyl)ethanol + O2
?
-
-
-
-
?
1-(4'-Hydroxyphenyl)-2-butanone + O2
?
2-(4'-Hydroxyphenyl)ethanol + O2
?
-
-
-
-
?
2-amino-p-cresol + O2
?
-
-
-
?
2-Methoxy-4-n-propylphenol + O2
1-(4'-Hydroxy-3'-methoxyphenyl)propanol
2-methyl-p-cresol + O2
?
-
-
-
?
3-(4'-Hydroxyphenyl)propanol + O2
?
-
-
-
-
?
3-methoxy-4-hydroxybenzyl alcohol + O2
3-methoxy-4-hydroxybenzaldehyde + H2O2
-
i.e. vanillyl alcohol
i.e. vanillin
-
?
4-(3'-methylcrotyl)phenol + O2
4-[(1E)-3-hydroxy-3-methylbut-1-en-1-yl]phenol + 4-[(1E)-3-methylbuta-1,3-dien-1-yl]phenol
4-(methoxymethyl)phenol + O2
?
4-(methoxymethyl)phenol + O2
? + H2O2
-
-
-
?
4-(methoxymethyl)phenol + O2 + H2O
4-hydroxybenzaldehyde + methanol + H2O2
4-butylphenol + O2
4-but-1-en-1-ylphenol + 4-[(1R)-1-hydroxybutyl]phenol
-
-
mutant D170E: 0% alcohol + 100% alkene. Mutant D170S: 82% alcohol + 18% alkene
-
?
4-cyclohexylphenol + O2
?
-
-
-
?
4-cyclopentylphenol + O2
4-(1-cyclopenten-1-yl)phenol
-
-
-
?
4-ethylguaiacol + O2
? + H2O2
-
-
-
?
4-ethylphenol + O2
1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + 4-hydroxyacetophenone
4-ethylphenol + O2 + H2O
(R)-1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + H2O2
-
-
product formed by wild-type enzyme and mutant enzyme D170S. The hydroxylation reaction in D170S is nearly completely blocked and this mutant converts short-chain alkylphenols to the corresponding alkenes. Mutant D170E: 8% alcohol + 92% alkene. Mutant D170S: 92% alcohol + 8% alkene
-
?
4-ethylphenol + O2 + H2O
(R)-1-(4'-hydroxyphenyl)ethanol + H2O2
4-ethylphenol + O2 + H2O
(S)-1-(4'-hydroxyphenyl)ethanol + H2O2
-
predominant product of mutant D170S/T457E
-
ir
4-ethylphenol + O2 + H2O
1-(4'-hydroxyphenyl)ethanol + H2O2
-
-
-
?
4-ethylphenol + O2 + H2O
? + H2O2
-
-
-
?
4-hydroxy-3-methoxybenzylamine + O2 + H2O
vanillin + H2O2 + NH3
-
i.e. vanillylamine
-
-
?
4-hydroxy-3-methoxyphenylglycol + O2 + H2O
2-hydroxy-1-(4-hydroxy-3-methoxyphenyl)ethan-1-one + H2O2
-
-
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
at 75% of the activity with vanillyl alcohol
-
?
4-isopropylphenol + O2
4-(2-hydroxypropan-2-yl)phenol + 4-isopropenylphenol
-
-
20% 4-hydroxyphenylalcohol + 80% 4-hydroxyphenylalkene
?
4-isopropylphenol + O2
4-isopropenylphenol + ?
-
-
mutant D170E: 8% alcohol + 92% alkene. Mutant D170S: 80% alcohol + 20% alkene
-
?
4-Methylphenol + O2
?
-
transient intermediate: p-quinone methide of the aromatic substrate in complex with reduced enzyme. Ordered sequential binding mechanism in which the rate of flavin reduction determines the turnover rate while the reduced enzyme-p-quinone methide binary complex rapidly reacts with dioxygen
-
-
?
4-n-butylphenol + O2
4-[(1E)-but-1-en-1-yl]phenol + 4-[(1Z)-but-1-en-1-yl]phenol
-
-
93% cis-4-hydroxyphenylalkene + 7% trans-4-hydroxyphenylalkene
?
4-n-heptylphenol + O2
4-[(1E)-hept-1-en-1-yl]phenol + 4-[(1Z)-hept-1-en-1-yl]phenol
-
-
50% cis-4-hydroxyphenylalkene + 50% trans-4-hydroxyphenylalkene
?
4-n-pentylphenol + O2
4-[(1E)-pent-1-en-1-yl]phenol + 4-[(1Z)-pent-1-en-1-yl]phenol + H2O2
4-n-propylphenol + O2
1-(4'-hydroxyphenyl)propanol + 4-(prop-1-en-1-yl)phenol
-
-
mutant D170E: 7% alcohol + 93% alkene. Mutant D170S: 96% alcohol + 4% alkene
-
?
4-n-propylphenol + O2
?
-
-
-
?
4-propylphenol + O2
(R)-1-(4'-hydroxyphenyl)propanol + cis-1-(4'-hydroxyphenyl)propene + trans-1-(4'-hydroxyphenyl)propene
-
-
in an aqueous medium the enzyme produces mainly (R)-1-(4'-hydroxyphenyl)propanol and low but equal amounts of cis-1-(4'-hydroxyphenyl)propene and trans-1-(4'-hydroxyphenyl)propene. In acetonitrile or toluene the concentration of the alcohol product decreases and the concentration of the cis-alkene product, but not the trans-alkene product increases
-
?
4-Propylphenol + O2
1-(4'-Hydroxyphenyl)propanol + 4-propenylphenol + 1-(4'-hydroxyphenyl)propanone
4-sec-butylphenol + O2
4-(2-hydroxybutan-2-yl)phenol + 4-(but-1-en-2-yl)phenol + 4-[(2Z)-but-2-en-2-yl]phenol
-
-
26% 4-hydroxyphenylalcohol + 74% 4-hydroxyphenylalkene. 100% cis-4-hydroxyphenylalkene
?
4-sec-butylphenol + O2
?
-
-
mutant D170E: 1% alcohol + 99% alkene. Mutant D170S: 78% alcohol + 22% alkene
-
?
5,6,7,8-tetrahydro-2-naphthol + O2
?
-
-
4% 4-hydroxyphenylalcohol + 94% 4-hydroxyphenylalkene + 2% 4-hydroxyphenylalkanone
?
5-indanol + O2
?
-
-
16% 4-hydroxyphenylalcohol + 24% 4-hydroxyphenylalkene + 60% 4-hydroxyphenylalkanone
?
5-indanol + O2
? + H2O2
-
-
-
?
chavicol + O2 + H2O
coumaryl alcohol + H2O2
creosol + O2
vanillin + ?
-
the conversion of cresol proceeds via a two-step enzymatic process. In the first step creosol is hydroxylated to yield vanillyl alcohol, and in the second step vanillyl alcohol is oxidized to yield vanillin
-
-
?
creosol + O2
vanillin + H2O
-
-
-
?
eugenol + O2 + H2O
coniferyl alcohol + H2O2
metanephrine + O2
?
-
-
-
-
?
norepinephrine + O2
?
-
-
-
-
?
normetanephrine + O2
?
-
-
-
-
?
propylphenol + O2
?
-
-
-
-
r
vanillyl alcohol + O2
?
-
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
vanillyl alcohol + phenazine methosulfate
vanillin + reduced phenazine methosulfate
-
-
-
?
vanillylamine + O2
?
-
-
-
-
?
vanillylamine + O2
? + H2O2
-
-
-
?
additional information
?
-
1-(4'-Hydroxyphenyl)-2-butanone + O2
?
-
-
-
-
?
1-(4'-Hydroxyphenyl)-2-butanone + O2
?
-
i.e., frambinon
-
-
r
2-Methoxy-4-n-propylphenol + O2
1-(4'-Hydroxy-3'-methoxyphenyl)propanol
-
-
94% R-enantiomer of 1-(4'-hydroxy-3'-methoxyphenyl)propanol
?
2-Methoxy-4-n-propylphenol + O2
1-(4'-Hydroxy-3'-methoxyphenyl)propanol
-
-
90% 4-hydroxyphenylalcohol + 10% 4-hydroxyphenylalkene. Less than 1% cis-4-hydroxyphenylalkene + more than 99% trans-4-hydroxyphenylalkene
?
4-(3'-methylcrotyl)phenol + O2
4-[(1E)-3-hydroxy-3-methylbut-1-en-1-yl]phenol + 4-[(1E)-3-methylbuta-1,3-dien-1-yl]phenol
-
-
-
-
?
4-(3'-methylcrotyl)phenol + O2
4-[(1E)-3-hydroxy-3-methylbut-1-en-1-yl]phenol + 4-[(1E)-3-methylbuta-1,3-dien-1-yl]phenol
-
-
40% 4-hydroxyphenylalcohol + 60% 4-hydroxyphenylalkene. 100% trans-4-hydroxyphenylalkene
?
4-(methoxymethyl)phenol + O2
?
-
-
-
-
?
4-(methoxymethyl)phenol + O2
?
-
-
-
?
4-(methoxymethyl)phenol + O2 + H2O
4-hydroxybenzaldehyde + methanol + H2O2
-
-
-
-
?
4-(methoxymethyl)phenol + O2 + H2O
4-hydroxybenzaldehyde + methanol + H2O2
-
like native enzyme the mutant enzymes T457E, D170A and d170S preferentially form the (R)-enantiomer. The mutant enzymes D170A/T457E and D170S/T457E exhibit an inverted stereospecificity
-
?
4-(methoxymethyl)phenol + O2 + H2O
4-hydroxybenzaldehyde + methanol + H2O2
-
upon reduction, a binary complex is produced composed of the p-quinone methide of 4-(methoxymethyl)phenol and reduced enzyme
-
?
4-ethylphenol + O2
1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + 4-hydroxyacetophenone
-
-
76% 4-hydroxyphenolalcohol + 24% 4-hydroxyphenylalkene
?
4-ethylphenol + O2
1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + 4-hydroxyacetophenone
-
-
94% R-enantiomer of 1-(4'-hydroxyphenyl)ethanol. 78% 1-(4'-hydroxyphenyl)ethanol + 18% 4-vinylphenol + 4% 4-hydroxyacetophenone
?
4-ethylphenol + O2
1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + 4-hydroxyacetophenone
-
transient intermediate: p-quinone methide of the aromatic substrate in complex with reduced enzyme. Ordered sequential binding mechanism in which the rate of flavin reduction determines the turnover rate while the reduced enzyme-p-quinone methide binary complex rapidly reacts with dioxygen
-
-
?
4-ethylphenol + O2 + H2O
(R)-1-(4'-hydroxyphenyl)ethanol + H2O2
-
-
product formed by wild-type enzyme and mutant enzymes D170S and D170A.D170A/T457E and D170S/T457E form (S)-1-(4'-hydroxyphenyl)ethanol. The hydroxylation reaction in D170S is nearly completely blocked and this mutant converts short-chain alkylphenols to the corresponding alkenes. Mutant D170E: 8% alcohol + 92% alkene. Mutant D170S: 92% alcohol + 8% alkene
-
?
4-ethylphenol + O2 + H2O
(R)-1-(4'-hydroxyphenyl)ethanol + H2O2
-
predominant product of wild-type enzyme and of mutant T457E
-
ir
4-n-pentylphenol + O2
4-[(1E)-pent-1-en-1-yl]phenol + 4-[(1Z)-pent-1-en-1-yl]phenol + H2O2
-
-
-
-
?
4-n-pentylphenol + O2
4-[(1E)-pent-1-en-1-yl]phenol + 4-[(1Z)-pent-1-en-1-yl]phenol + H2O2
-
-
60% cis-4-hydroxyphenylalkene + 40% trans-4-hydroxyphenylalkene
?
4-Propylphenol + O2
1-(4'-Hydroxyphenyl)propanol + 4-propenylphenol + 1-(4'-hydroxyphenyl)propanone
-
-
-
-
?
4-Propylphenol + O2
1-(4'-Hydroxyphenyl)propanol + 4-propenylphenol + 1-(4'-hydroxyphenyl)propanone
-
-
-
-
r
4-Propylphenol + O2
1-(4'-Hydroxyphenyl)propanol + 4-propenylphenol + 1-(4'-hydroxyphenyl)propanone
-
-
94% R-enantiomer of 1-(4'-hydroxyphenyl)propanol. 78% 1-(4'-hydroxyphenyl)propanol + 18% 4-propenylphenol + 4% 1-(4'-hydroxyphenyl)propanone
?
4-Propylphenol + O2
1-(4'-Hydroxyphenyl)propanol + 4-propenylphenol + 1-(4'-hydroxyphenyl)propanone
-
4-n-propylphenol
45% cis-4-hydroxyphenylalkene + 55% trans-4-hydroxyphenylalkene
?
chavicol + O2 + H2O
coumaryl alcohol + H2O2
-
-
-
?
chavicol + O2 + H2O
coumaryl alcohol + H2O2
-
-
-
?
eugenol + O2
?
-
-
-
-
?
eugenol + O2 + H2O
coniferyl alcohol + H2O2
-
-
-
?
eugenol + O2 + H2O
coniferyl alcohol + H2O2
-
-
-
-
?
eugenol + O2 + H2O
coniferyl alcohol + H2O2
-
-
-
?
eugenol + O2 + H2O
coniferyl alcohol + H2O2
-
-
-
-
?
p-cresol + O2
?
-
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
-
?
vanillyl alcohol + O2
vanillin + H2O2
-
-
-
?
additional information
?
-
-
enzyme also catalyzes the oxidative deamination of 4-hydroxybenzylamines and the oxidative demethylation of 4-(methoxymethyl)phenols
-
-
?
additional information
?
-
-
short-chain 4-alkylphenols are predominantly hydroxylated to (R)-1-(4'-hydroxyphenyl) alcohols, whereas medium-chain 4-alkylphenols are dehydrogenated to the corresponding 1-(4'-hydroxyphenyl) alkenes
-
-
?
additional information
?
-
covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process
-
-
?
additional information
?
-
enzyme also oxidizes eugenol. Poor substrates: vanillylamine, 4-ethylguaiacol
-
-
-
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Amblyopia
Epidemiology and intermediate-term outcomes of open- and closed-globe injuries in traumatic childhood cataract.
Amblyopia
Visual Axis Opacification in Children Following Paediatric Cataract Surgery.
Aniridia
The efficacy and complications of black diaphragm intra-ocular lens implantation in patients with congenital aniridia.
Aphakia
Management of Aphakia with Visual Axis Opacification after Congenital Cataract Surgery Based on UBM Image Features Analysis.
Aphakia
[Congenital cataracts: complications and functional results according to different surgical techniques]
Asthma
Dynamic Respiratory Tortuosity of the Vertebral Artery Ostium.
Astigmatism
Visual outcomes after toric intraocular lens implantation in pediatric eyes undergoing cataract surgery.
Carotid Stenosis
Prevalence and Prognosis of Asymptomatic Vertebral Artery Origin Stenosis in Patients With Clinically Manifest Arterial Disease.
Carotid Stenosis
Prevalence of vertebral artery origin stenosis and occlusion in outpatient extracranial ultrasonography.
Cataract
Capsular opacification after vitreous-sparing cataract surgery in children.
Cataract
Epidemiology and intermediate-term outcomes of open- and closed-globe injuries in traumatic childhood cataract.
Cataract
Management of Aphakia with Visual Axis Opacification after Congenital Cataract Surgery Based on UBM Image Features Analysis.
Cataract
Outcomes of Bilateral Cataract Surgery in Infants 7 to 24 Months of Age Using the Toddler Aphakia and Pseudophakia Treatment Study Registry.
Cataract
Phacoemulsification and primary implantation with bag-in-the-lens intraocular lens in children with unilateral and bilateral cataract.
Cataract
Visual Axis Opacification in Children Following Paediatric Cataract Surgery.
Cataract
Visual Axis Opacity after Intraocular Lens Implantation in Children in the First 2 Years of Life: Findings from the IoLunder2 Cohort Study.
Congenital Abnormalities
The first 50 live births after autologous oocyte vitrification in France.
Cough
Antitussive, expectorant, and bronchodilating effects of quinazoline alkaloids (±)-vasicine, deoxyvasicine, and (±)-vasicinone from aerial parts of Peganum harmala L.
Embolic Stroke
Cryptic Recanalization of Chronic Vertebral Artery Occlusion by Head Rotation.
Glaucoma
Glaucoma in aphakic and pseudophakic eyes following surgery for congenital cataract in the first year of life.
Glaucoma
Intraoperative performance and postoperative outcomes of cataract surgery in infant eyes with microphthalmos.
Glaucoma
Outcomes of Bilateral Cataract Surgery in Infants 7 to 24 Months of Age Using the Toddler Aphakia and Pseudophakia Treatment Study Registry.
Glaucoma
Postoperative outcomes of intraocular lens implantation in the bag versus posterior optic capture in pediatric cataract surgery.
Glaucoma
Second intraocular surgery after primary pediatric cataract surgery: indications and outcomes during long-term follow-up at a tertiary eye care center.
Glaucoma
Secondary intraocular lens implantation following infantile cataract surgery: intraoperative indications, postoperative outcomes.
Glaucoma
The efficacy and complications of black diaphragm intra-ocular lens implantation in patients with congenital aniridia.
Glaucoma
Visual outcomes after toric intraocular lens implantation in pediatric eyes undergoing cataract surgery.
Hypercholesterolemia
Effect of virgin avocado oil on diet-induced hypercholesterolemia in rats via 1 H NMR-based metabolomics approach.
Ischemic Stroke
Cryptic Recanalization of Chronic Vertebral Artery Occlusion by Head Rotation.
Ischemic Stroke
Long-term outcome of vertebral artery origin stenosis in patients with acute ischemic stroke.
Ischemic Stroke
Prevalence and Prognosis of Asymptomatic Vertebral Artery Origin Stenosis in Patients With Clinically Manifest Arterial Disease.
Kidney Failure, Chronic
Consumption of Argan Oil Improves Anti-Oxidant and Lipid Status in Hemodialysis Patients.
Myocardial Ischemia
Risk Factors for Restenosis After Stenting or Angioplasty of Vertebral Artery Origin : Results of Short-term and Long-term Follow-up.
Osteophyte
Cryptic Recanalization of Chronic Vertebral Artery Occlusion by Head Rotation.
Overweight
Risk Factors for Restenosis After Stenting or Angioplasty of Vertebral Artery Origin : Results of Short-term and Long-term Follow-up.
Pulmonary Disease, Chronic Obstructive
Dynamic Respiratory Tortuosity of the Vertebral Artery Ostium.
Pupil Disorders
Management of Aphakia with Visual Axis Opacification after Congenital Cataract Surgery Based on UBM Image Features Analysis.
Refractive Errors
A Comparison Between Refraction From an Adaptive Optics Visual Simulator and Clinical Refractions.
Stroke
Prevalence and Prognosis of Asymptomatic Vertebral Artery Origin Stenosis in Patients With Clinically Manifest Arterial Disease.
Stroke
Topography of Vertebral Artery Origin Plaques: Characteristics and Determinants.
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0.222
(R)-1-(4'-hydroxyphenol)ethanol
-
-
0.03
(R,S)-1-(4'-Hydroxyphenyl)propanol
-
-
0.026
(S)-1-(4'-hydroxyphenyl)ethanol
-
-
0.128
1-(4'-Hydroxyphenyl)-2-butanone
-
-
0.1
2-(4'-hydroxyphenyl)ethanol
-
-
0.029 - 0.254
2-amino-p-cresol
0.006
2-Methoxy-4-n-propylphenol
-
-
0.001 - 0.021
2-methyl-p-cresol
0.065
4-(3'-methylcrotyl)phenol
-
-
0.0023 - 238
4-(Methoxymethyl)phenol
0.006
4-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.0021
4-ethylguaiacol
pH 7.5, 25°C
-
0.007 - 0.048
4-Ethylphenol
0.24
4-Hydroxy-3-methoxybenzylamine
-
-
0.016 - 0.088
4-isopropylphenol
0.002
4-n-butylphenol
-
-
0.042
4-n-heptylphenol
-
-
0.008
4-n-pentylphenol
-
-
0.01
4-n-Propylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.003 - 0.004
4-Propylphenol
0.062 - 0.075
4-sec-butylphenol
0.094
5,6,7,8-tetrahydro-2-naphthol
-
-
0.031
p-Cresol
pH 7.5, 25°C, wild-type enzyme
0.043
phenazine methosulfate
-
-
0.006 - 1.75
Vanillyl alcohol
0.048 - 0.076
vanillylamine
additional information
additional information
-
-
0.029
2-amino-p-cresol
pH 10, 25°C, mutant enzyme T505S
0.043
2-amino-p-cresol
pH 10, 25°C, mutant enzyme E502G
0.05
2-amino-p-cresol
pH 10, 25°C, mutant enzyme I238T
0.064
2-amino-p-cresol
pH 10, 25°C, mutant enzyme F454Y
0.118
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme I238T
0.123
2-amino-p-cresol
pH 7.5, 25°C, wild-type enzyme
0.167
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme F454Y
0.2
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme E502G
0.254
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme T505S
0.001
2-methyl-p-cresol
pH 10, 25°C, mutant enzyme E502G
0.006
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme F454Y
0.007
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme E502G
0.007
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme T505S
0.017
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme I238T
0.021
2-methyl-p-cresol
pH 7.5, 25°C, wild-type enzyme
0.0023
4-(Methoxymethyl)phenol
pH 7.5, 25°C
0.004
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme E502G
0.014
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme T505S
0.02
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme I238T
0.023
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme F454Y
0.033
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme T505S
0.034
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422A
0.037
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422C
0.04
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H61T
0.041
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422T
0.051
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme I238T
0.054
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme F454Y
0.058
4-(Methoxymethyl)phenol
pH 7.5, 25°C, wild-type enzyme
0.064
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme E502G
0.11
4-(Methoxymethyl)phenol
pH 10, 25°C, wild-type enzyme
0.113
4-(Methoxymethyl)phenol
-
pH 7.5, 25°C, mutant enzyme D170E
55
4-(Methoxymethyl)phenol
pH 7.5, 25°Cm wild-type enzyme
65
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme D170A/T457E
168
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme T457E
238
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme D170S/T457E
0.007
4-Ethylphenol
-
-
0.012
4-Ethylphenol
wild type enzyme, at pH 7.5 and 25°C
0.048
4-Ethylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.016
4-isopropylphenol
-
-
0.026
4-isopropylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.088
4-isopropylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.003
4-Propylphenol
-
-
0.0037
4-Propylphenol
-
-
0.062
4-sec-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.072
4-sec-butylphenol
-
-
0.075
4-sec-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.0048
chavicol
-
-
0.0065
chavicol
wild-type, pH 7.5, 25°C
0.021
chavicol
mutant Y503F, pH 7.5, 25°C
0.067
chavicol
mutant Y108F, pH 7.5, 25°C
0.074
chavicol
mutant Y108F/Y503F, pH 7.5, 25°C
0.001
creosol
pH 10, 25°C, mutant enzyme I238T
0.001
creosol
pH 10, 25°C, mutant enzyme T505S
0.002
creosol
pH 10, 25°C, mutant enzyme F454Y
0.002
creosol
pH 10, 25°C, wild-type enzyme
0.013
creosol
pH 7.5, 25°C, mutant enzyme F454Y
0.02
creosol
pH 7.5, 25°C, wild-type enzyme
0.027
creosol
pH 7.5, 25°C, mutant enzyme E502G
0.031
creosol
pH 7.5, 25°C, mutant enzyme T505S
0.041
creosol
pH 7.5, 25°C, mutant enzyme I238T
0.05
creosol
-
pH 7.4, 25°C
0.0002
eugenol
pH 10, 25°C, mutant enzyme I238T
0.0008
eugenol
pH 10, 25°C, mutant enzyme F454Y
0.0008
eugenol
pH 7.5, 25°C, mutant enzyme T505S
0.002
eugenol
pH 7.5, 25°C, wild-type enzyme
0.002
eugenol
pH 10, 25°C, mutant enzyme T505S
0.002
eugenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.002
eugenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.003
eugenol
pH 7.5, 25°C, mutant enzyme F454Y
0.0039
eugenol
wild type enzyme, at pH 7.5 and 25°C
0.005
eugenol
pH 7.5, 25°C, mutant enzyme E502G
0.008
eugenol
pH 7.5, 25°C, mutant enzyme I238T
0.019
eugenol
pH 10, 25°C, wild-type enzyme
0.006
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme T505S
0.007
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme F454Y
0.007
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme I238T
0.01
Vanillyl alcohol
pH 10, 25°C, mutant enzyme E502G
0.01
Vanillyl alcohol
pH 10, 25°C, mutant enzyme T505S
0.015
Vanillyl alcohol
pH 10, 25°C, mutant enzyme F454Y
0.022
Vanillyl alcohol
pH 10, 25°C, mutant enzyme I238T
0.04
Vanillyl alcohol
pH 7.5, 25°C
0.051
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme E502G
0.075
Vanillyl alcohol
pH 7.5, 25°C, wild-type enzyme
0.129
Vanillyl alcohol
His-tagged recombinant enzyme, pH 7.5, 25°C
0.149
Vanillyl alcohol
wild-type, pH 7.5, 25°C
0.149
Vanillyl alcohol
wild type enzyme, at pH 7.5 and 25°C
0.189
Vanillyl alcohol
pH 10, 25°C, wild-type enzyme
0.2
Vanillyl alcohol
-
pH 7, 25°C
0.29
Vanillyl alcohol
-
-
0.34
Vanillyl alcohol
-
pH 7.5, 25°C, mutant enzyme D170E
0.5
Vanillyl alcohol
pH 7, 25°C
0.73
Vanillyl alcohol
-
-
0.99
Vanillyl alcohol
mutant Y503F, pH 7.5, 25°C
1.75
Vanillyl alcohol
mutant Y108F, pH 7.5, 25°C
0.048
vanillylamine
-
pH 7.4, 25°C
0.076
vanillylamine
pH 7.5, 25°C
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0.7
(R)-1-(4'-hydroxyphenol)ethanol
-
-
3
(R,S)-1-(4'-Hydroxyphenyl)propanol
-
-
4.4
(S)-1-(4'-hydroxyphenyl)ethanol
-
-
0.3
1-(4'-Hydroxyphenyl)-2-butanone
-
-
0.004
2-(4'-hydroxyphenyl)ethanol
-
-
0.001 - 0.099
2-amino-p-cresol
3.2
2-Methoxy-4-n-propylphenol
-
-
4.8
2-methoxy-4-propylphenol
-
-
0.002 - 0.063
2-methyl-p-cresol
0.1
3-(4'-hydroxyphenol)propanol
-
-
1.4
4-(3'-methylcrotyl)phenol
-
-
5.3
4-(methoxymethyl)-phenol
-
-
0.002 - 3.9
4-(Methoxymethyl)phenol
0.0001 - 0.12
4-butylphenol
3.7
4-cyclopentylphenol
His-tagged recombinant enzyme, pH 7.5, 25°C
-
0.026
4-ethylguaiacol
pH 7.5, 25°C
-
0.0001 - 2.7
4-Ethylphenol
1.3
4-Hydroxy-3-methoxybenzylamine
-
-
3.6
4-hydroxy-3-methoxyphenylglycol
-
-
0.13 - 1.3
4-isopropylphenol
0.0002 - 4.2
4-n-Propylphenol
0.05 - 0.5
4-sec-butylphenol
0.7
5,6,7,8-tetrahydro-2-naphthol
-
-
0.0002
p-Cresol
-
pH 7.5, 25°C, mutant enzyme D170E
0.26
propylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.004 - 19.5
Vanillyl alcohol
0.02 - 0.26
vanillylamine
0.001
2-amino-p-cresol
pH 10, 25°C, wild-type enzyme
0.017
2-amino-p-cresol
pH 7.5, 25°C, wild-type enzyme
0.046
2-amino-p-cresol
pH 10, 25°C, mutant enzyme T505S
0.047
2-amino-p-cresol
pH 10, 25°C, mutant enzyme F454Y
0.076
2-amino-p-cresol
pH 10, 25°C, mutant enzyme E502G
0.079
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme I238T
0.082
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme F454Y
0.086
2-amino-p-cresol
pH 10, 25°C, mutant enzyme I238T
0.087
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme T505S
0.099
2-amino-p-cresol
pH 7.5, 25°C, mutant enzyme E502G
0.002
2-methyl-p-cresol
pH 10, 25°C, wild-type enzyme
0.01
2-methyl-p-cresol
pH 10, 25°C, mutant enzyme F454Y
0.019
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme E502G
0.02
2-methyl-p-cresol
pH 10, 25°C, mutant enzyme I238T
0.023
2-methyl-p-cresol
pH 10, 25°C, mutant enzyme T505S
0.025
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme T505S
0.028
2-methyl-p-cresol
pH 10, 25°C, mutant enzyme E502G
0.031
2-methyl-p-cresol
pH 7.5, 25°C, wild-type enzyme
0.032
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme F454Y
0.063
2-methyl-p-cresol
pH 7.5, 25°C, mutant enzyme I238T
0.002
4-(Methoxymethyl)phenol
-
pH 7.5, 25°C, mutant enzyme D170N
0.004
4-(Methoxymethyl)phenol
pH 7.5, 25°C
0.004
4-(Methoxymethyl)phenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.02
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme D170A/T457E
0.05
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme D170S/T457E
0.07
4-(Methoxymethyl)phenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.24
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H61T
0.27
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422A
0.28
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422T
0.32
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme H422C
1.1
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme E502G
1.2
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme E502G
1.3
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme T457E
2.1
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme F454Y
2.1
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme I238T
2.3
4-(Methoxymethyl)phenol
pH 7.5, 25°C, mutant enzyme T505S
3
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme I238T
3.1
4-(Methoxymethyl)phenol
pH 7.5, 25°C, wild-type enzyme
3.1
4-(Methoxymethyl)phenol
pH 7.5, 25°Cm wild-type enzyme
3.4
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme F454Y
3.6
4-(Methoxymethyl)phenol
pH 10, 25°C, mutant enzyme T505S
3.9
4-(Methoxymethyl)phenol
pH 10, 25°C, wild-type enzyme
0.0001
4-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.12
4-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.0001
4-Ethylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.17
4-Ethylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
2.6
4-Ethylphenol
wild type enzyme, at pH 7.5 and 25°C
0.13
4-isopropylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.18
4-isopropylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
1.3
4-isopropylphenol
-
-
0.0002
4-n-Propylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.05
4-sec-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.09
4-sec-butylphenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.5
4-sec-butylphenol
-
-
0.13
chavicol
mutant Y108F/Y503F, pH 7.5, 25°C
3.3
chavicol
mutant Y503F, pH 7.5, 25°C
3.4
chavicol
mutant Y108F, pH 7.5, 25°C
7.4
chavicol
wild-type, pH 7.5, 25°C
0.003
creosol
pH 8, 25°C, wild-type enzyme
0.005
creosol
pH 10, 25°C, wild-type enzyme
0.01
creosol
pH 8, 25°C, mutant enzyme T505S
0.013
creosol
pH 10, 25°C, mutant enzyme F454Y
0.013
creosol
pH 8, 25°C, wild-type enzyme
0.015
creosol
pH 10, 25°C, mutant enzyme A429V
0.015
creosol
pH 8, 25°C, mutant enzyme I237T/M437L
0.016
creosol
pH 8, 25°C, mutant enzyme E502G
0.017
creosol
pH 10, 25°C, mutant enzyme T505S
0.017
creosol
pH 8, 25°C, mutant enzyme F454Y
0.018
creosol
pH 8, 25°C, mutant enzyme A429V
0.019
creosol
pH 10, 25°C, mutant enzyme F93Y/P189S/I238T
0.02
creosol
pH 7.5, 25°C, wild-type enzyme
0.02
creosol
pH 10, 25°C, mutant enzyme E502G
0.02
creosol
pH 10, 25°C, mutant enzyme I238T
0.021
creosol
pH 10, 25°C, mutant enzyme I237T/M437L
0.022
creosol
pH 8, 25°C, mutant enzyme I238T
0.07
creosol
-
pH 7.4, 25°C
0.07
creosol
pH 10, 25°C, mutant enzyme I238T
0.09
creosol
pH 10, 25°C, mutant enzyme E502G
0.1
creosol
pH 10, 25°C, mutant enzyme F454Y
0.1
creosol
pH 10, 25°C, mutant enzyme T505S
0.1
creosol
pH 7.5, 25°C, mutant enzyme E502G
0.12
creosol
pH 7.5, 25°C, mutant enzyme T505S
0.14
creosol
pH 7.5, 25°C, mutant enzyme F454Y
0.17
creosol
pH 7.5, 25°C, mutant enzyme I238T
0.01
eugenol
-
pH 7.5, 25°C, mutant enzyme D170S
0.1
eugenol
pH 10, 25°C, mutant enzyme E502G
0.17
eugenol
pH 7.5, 25°C, mutant enzyme E502G
0.23
eugenol
pH 10, 25°C, mutant enzyme F454Y
0.34
eugenol
-
pH 7.5, 25°C, mutant enzyme D170E
0.5
eugenol
pH 7.5, 25°C, mutant enzyme F454Y
0.55
eugenol
pH 10, 25°C, mutant enzyme T505S
0.6
eugenol
pH 10, 25°C, mutant enzyme I238T
0.65
eugenol
pH 7.5, 25°C, mutant enzyme T505S
0.8
eugenol
pH 7.5, 25°C, mutant enzyme I238T
11
eugenol
wild type enzyme, at pH 7.5 and 25°C
14
eugenol
pH 7.5, 25°C, wild-type enzyme
39
eugenol
pH 10, 25°C, wild-type enzyme
0.004
Vanillyl alcohol
-
pH 7.5, 25°C, mutant enzyme D170S
0.042
Vanillyl alcohol
mutant Y108F, pH 7.5, 25°C
0.055
Vanillyl alcohol
mutant Y503F, pH 7.5, 25°C
0.21
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme T505S
0.22
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme E502G
0.25
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme F454Y
0.3
Vanillyl alcohol
pH 10, 25°C, mutant enzyme E502G
0.39
Vanillyl alcohol
pH 7.5, 25°C, mutant enzyme I238T
0.67
Vanillyl alcohol
pH 10, 25°C, mutant enzyme T505S
0.71
Vanillyl alcohol
pH 10, 25°C, mutant enzyme F454Y
1.3
Vanillyl alcohol
-
pH 7.5, 25°C, mutant enzyme D170E
1.4
Vanillyl alcohol
pH 10, 25°C, mutant enzyme I238T
1.6
Vanillyl alcohol
pH 7.5, 25°C, wild-type enzyme
2.4
Vanillyl alcohol
pH 10, 25°C, wild-type enzyme
2.5
Vanillyl alcohol
His-tagged recombinant enzyme, pH 7.5, 25°C
2.6
Vanillyl alcohol
wild-type, pH 7.5, 25°C
2.6
Vanillyl alcohol
wild type enzyme, at pH 7.5 and 25°C
8
Vanillyl alcohol
-
pH 7, 25°C
12
Vanillyl alcohol
pH 7.5, 25°C
19.5
Vanillyl alcohol
pH 7, 25°C
0.02
vanillylamine
-
pH 7.4, 25°C
0.26
vanillylamine
pH 7.5, 25°C
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C470L
mutant displays similar activity to the wild-type enzyme with the substrates vanillyl alcohol, chavicol aund eugenol, but no activity with linear 4-alkylphenols
D170A/T457E
-
produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol
D170S/T457E
-
produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol
E502G
the octamer/dimer ratio is 1:10. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
F424G
mutant does not contain any flavin after purification
F454Y
as for wild-type enzyme the octamer/dimer ratio of the mutant enzyme is 1.5:1. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
H422A
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Mutant enzyme is still able to form a stable binary complex of reduced enzyme and a quinone methide product intermediate, a crucial step during vanillyl-alcohol oxidase-mediated catalysis. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
H422C
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
H422T
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
I238T
the octamer/dimer ratio is 4:1. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
I468V
mutant displays similar activity to the wild-type enzyme with the substrates vanillyl alcohol, chavicol aund eugenol, but no activity with linear 4-alkylphenols
L316M
mutant displays substrate specificity profile similar to wild-type
T457Q
mutant shows about 3fold increased activity towards vanillyl alcohol, but decrease in activity with all other substrates
T459I
mutant displays substrate specificity profile similar to wild-type
T505S
as for wild-type enzyme the octamer/dimer ratio of the mutant enzyme is 1.5:1
Y108F
deprotonation of the substrate's phenol group is impaired
Y108F/Y503F
deprotonation of the substrate's phenol group is impaired
Y503F
deprotonation of the substrate's phenol group is impaired
additional information
exchange of a loop at the dimer-dimer interface in octameric vanillin oxidase that is not present in dimeric EUGO. A vanillin oxidase variant where the loop was deleted, loopless VAO, exclusively forms dimers. Introduction of the loop into EUGO is not sufficient to induce its octamerization. Neither variant displays major changes in its catalytic properties as compared to the wild-type enzyme
D170A
-
3100fold decrease in turnover-number for for 4-(methoxymethyl)phenol
D170A
-
only 50% of the FAD is covalently bound. With vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme
D170E
-
2fold increase in KM-value for for 4-(methoxymethyl)phenol, 2.1fold increase in Km-value for vanillyl alcohol, 2fold decrease in KM-value for eugenol as compared to wild-type enzyme.442fold decrease in turnover-number for for 4-(methoxymethyl)phenol, 2.5fold decrease in turnover-number for vanillyl alcohol, 51.5fold decrease in turnover-number for eugenol as compared to wild-type enzyme.Redox potential of mutant enzyme, + 6 mV, is decreased compared to wild-type enzyme, 55 mV
D170E
-
substrate preference is similar to wild-type enzyme, as the wild-type enzyme the mutant enzyme favors the production of alkenes
D170E
-
with vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is 5-fold to 100fold less active than the wild-type enzyme
D170N
-
1550fold decrease in turnover-number for for 4-(methoxymethyl)phenol
D170N
-
no FAD is covalently bound. With vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme
D170S
-
2fold decrease in KM-value for eugenol as compared to wild-type enzyme.1290fold decrease in turnover-number for for 4-(methoxymethyl)phenol, 825fold decrease in turnover-number for vanillyl alcohol, 1750fold decrease in turnover-number for eugenol as compared to wild-type enzyme. Redox potential of mutant enzyme, -91 mV, is decreased compared to wild-type enzyme, 55 mV
D170S
-
most active with branched-chain 4-alkylphenol, mutant enzyme favors the formation of alcohols
D170S
-
with vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme
H61T
-
FAD-free apoenzyme H61T mainly exists as a dimeric species of 126000 Da. Binding of FAD to apoH61T rapidly restores enzyme activity and induces octamerization
H61T
in the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD and perform catalysis. The mutant enzyme is about 10fold less active with 4-(methoxymethyl)phenol than the wild-type enzyme. Crystal structure of both the holo and apo form of H61T are highly similar to the structure of the wild-type enzyme
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Van der Heuvel, R.H.H.; Fraaije, M.W.; Laane, C.; van Berkel, W.J.H.
Regio- and stereospecific conversion of 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase
J. Bacteriol.
180
5646-5651
1998
Penicillium simplicissimum
brenda
Fraaije, M.W.; Veeger, C.; van Berkel, W.J.H.
Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols
Eur. J. Biochem.
234
271-277
1995
Penicillium simplicissimum
brenda
De Jong, E.; van Berkel, W.J.H.; van der Zwan, R.P.; de Bont, J.A.M.
Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD
Eur. J. Biochem.
208
651-657
1992
Penicillium simplicissimum
brenda
Fraaije, M.W.; Sjollema, K.A.; Veenhuis, M.; van Berkel, W.J.H.
Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum
FEBS Lett.
422
65-68
1998
Penicillium simplicissimum
brenda
Fraaije, M.W.; Mattevi, A.; van Berkel, W.J.H.
Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers
FEBS Lett.
402
33-35
1997
Penicillium simplicissimum
brenda
Fraaije, M.W.; van Berkel, W.J.H.
Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediate
J. Biol. Chem.
272
18111-18116
1997
Penicillium simplicissimum
brenda
Fraaije, M.W.; van der Heuvel, R.H.H.; Roelofs, J.C.A.A.; van Berkel, W.J.H.
Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4-alkylphenols
Eur. J. Biochem.
253
712-719
1998
Penicillium simplicissimum
brenda
Drijfhout, F.P.; Fraaije, M.W.; Jongejan, H.; van Berkel, W.J.H.; Franssen, M.C.R.
Enantioselective hydroxylation of 4-alkylphenols by vanillyl alcohol oxidase
Biotechnol. Bioeng.
59
171-177
1998
Penicillium simplicissimum
brenda
Mattevi, A.; Fraaije, M.W.; Mozzarelli, A.; Olivi, L.; Coda, A.; van Berkel, W.J.H.
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity
Structure
5
907-920
1997
Penicillium simplicissimum
brenda
Benen, J.A.E.; Sanchez-Torres, P.; Wagemaker, M.J.; Fraaije, M.W.; van Berkel, W.J.; Visser, J.
Molecular cloning, sequencing, and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase
J. Biol. Chem.
273
7865-7872
1998
Penicillium simplicissimum (P56216), Penicillium simplicissimum, Penicillium simplicissimum CBS170.90 (P56216), Penicillium simplicissimum CBS170.90
brenda
Mattevi, A.; Fraaije, M.W.; Coda, A.; van Berkel, W.J.
Crystallization and preliminary X-ray analysis of the flavoenzyme vanilly-alcohol oxidase from Penicillium simplicissimum
Proteins
27
601-603
1997
Penicillium simplicissimum
brenda
van den Heuvel, R.H.H.; Laane, C.; van Berkel, W.J.H.
Exploring the biocatalytic potential of vanillyl-alcohol oxidase by site-directed mutagenesis
Adv. Synth. Catal.
343
515-520
2001
Penicillium simplicissimum
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brenda
van den Heuvel, R.H.; Fraaije, M.W.; van Berkel, W.J.
Direction of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols
FEBS Lett.
481
109-112
2000
Penicillium simplicissimum
brenda
van den Heuvel, R.H.; Partridge, J.; Laane, C.; Halling, P.J.; van Berkel, W.J.
Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering
FEBS Lett.
503
213-216
2001
Penicillium simplicissimum
brenda
van den Heuvel, R.H.; Fraaije, M.W.; Laane, C.; van Berkel, W.J.
Enzymatic synthesis of vanillin
J. Agric. Food Chem.
49
2954-2958
2001
Penicillium simplicissimum
brenda
Fraaije, M.W.; van den Heuvel, R.H.; van Berkel, W.J.; Mattevi, A.
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase
J. Biol. Chem.
274
35514-35520
1999
Penicillium simplicissimum (P56216)
brenda
van den Heuvel, R.H.; Fraaije, M.W.; Mattevi, A.; van Berkel, W.J.
Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase
J. Biol. Chem.
275
14799-14808
2000
Penicillium simplicissimum
brenda
Fraaije, M.W.; van den Heuvel, R.H.; van Berkel, W.J.; Mattevi, A.
Structural analysis of flavinylation in vanillyl-alcohol oxidase
J. Biol. Chem.
275
38654-38658
2000
Penicillium simplicissimum (P56216)
brenda
Tahallah, N.; van den Heuvel, R.H.; van den Berg, W.A.; Maier, C.S.; van Berkel, W.J.; Heck, A.J.
Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase
J. Biol. Chem.
277
36425-36432
2002
Penicillium simplicissimum
brenda
van den Heuvel, R.H.; van den Berg, W.A.; Rovida, S.; van Berkel, W.J.
Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin
J. Biol. Chem.
279
33492-33500
2004
Penicillium simplicissimum (P56216)
brenda
van den Heuvel, R.H.; Fraaije, M.W.; Ferrer, M.; Mattevi, A.; van Berkel, W.J.
Inversion of stereospecificity of vanillyl-alcohol oxidase
Proc. Natl. Acad. Sci. USA
97
9455-9460
2000
Penicillium simplicissimum (P56216)
brenda
Overhage, J.; Steinbuechel, A.; Priefert, H.
Harnessing eugenol as a substrate for production of aromatic compounds with recombinant strains of Amycolatopsis sp. HR167
J. Biotechnol.
125
369-376
2006
Penicillium simplicissimum, Penicillium simplicissimum CBS 170.90
brenda
Jin, J.; Mazon, H.; van den Heuvel, R.H.; Heck, A.J.; Janssen, D.B.; Fraaije, M.W.
Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process
FEBS J.
275
5191-5200
2008
Penicillium simplicissimum (P56216)
brenda
Ewing, T.A.; Gygli, G.; van Berkel, W.J.
A single loop is essential for the octamerization of vanillyl alcohol oxidase
FEBS J.
283
2546-2559
2016
Penicillium simplicissimum (P56216)
brenda
Vinambres, M.; Espada, M.; Martinez, A.T.; Serrano, A.
Screening and evaluation of new hydroxymethylfurfural oxidases for furandicarboxylic acid production
Appl. Environ. Microbiol.
86
e00842
2020
Pseudomonas sp. 11/12A, Methylovorus sp. MP688 (E4QP00)
brenda
Colpa, D.I.; Loncar, N.; Schmidt, M.; Fraaije, M.W.
Creating oxidase-peroxidase fusion enzymes as a toolbox for cascade reactions
Chembiochem
18
2226-2230
2017
Rhodococcus jostii (Q0SBK1)
brenda
Jin, J.; Mazon, H.; van den Heuvel, R.H.H.; Janssen, D.B.; Fraaije, M.W.
Discovery of a eugenol oxidase from Rhodococcus sp. strain RHA1
FEBS J.
274
2311-2321
2007
Rhodococcus jostii (Q0SBK1)
brenda
Ewing, T.A.; Gygli, G.; van Berkel, W.J.H.
A single loop is essential for the octamerization of vanillyl alcohol oxidase
FEBS J.
283
2546-2559
2016
Penicillium simplicissimum (P56216)
brenda
Ewing, T.A.; Nguyen, Q.T.; Allan, R.C.; Gygli, G.; Romero, E.; Binda, C.; Fraaije, M.W.; Mattevi, A.; van Berkel, W.J.H.
Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase
J. Biol. Chem.
292
14668-14679
2017
Penicillium simplicissimum (P56216), Penicillium simplicissimum
brenda
Ewing, T.A.; van Noord, A.; Paul, C.E.; van Berkel, W.J.H.
A xylenol orange-based screening assay for the substrate specificity of flavin-dependent para-phenol oxidases
Molecules
23
164
2018
Penicillium simplicissimum (P56216)
brenda
Gygli, G.; Lucas, M.F.; Guallar, V.; van Berkel, W.J.H.
The ins and outs of vanillyl alcohol oxidase Identification of ligand migration paths
PLoS Comput. Biol.
13
e1005787
2017
Penicillium simplicissimum (P56216)
brenda