Information on EC 1.1.1.90 - aryl-alcohol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.90
-
RECOMMENDED NAME
GeneOntology No.
aryl-alcohol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aromatic alcohol + NAD+ = an aromatic aldehyde + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
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-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,5-xylenol and 3,5-xylenol degradation
-
-
3-chlorotoluene degradation II
-
-
m-cresol degradation
-
-
m-xylene degradation to m-toluate
-
-
p-xylene degradation to p-toluate
-
-
salicin biosynthesis
-
-
salicortin biosynthesis
-
-
toluene degradation to benzoate
-
-
Tyrosine metabolism
-
-
Phenylalanine metabolism
-
-
Xylene degradation
-
-
Toluene degradation
-
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Metabolic pathways
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Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
aryl-alcohol:NAD+ oxidoreductase
A group of enzymes with broad specificity towards primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity towards short-chain aliphatic alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-26-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant strain H16(pBBR1-JO2ehyABcalAcalB)
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wheatgrass
-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
gene lp_3054
-
-
Manually annotated by BRENDA team
enzyme also capable of oxidizing aliphatic primary alcohols with NAD+
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-
Manually annotated by BRENDA team
rye
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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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SwissProt
Manually annotated by BRENDA team
Triticale turgidocereale
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
disruption mutant shows similar growth compared to wild-type
metabolism
-
the enzyme is involved in the metabolism of benzoic acid, proteomic analysis, overview
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-perillyl alcohol + NAD+
(R)-perillaldehyde + NADH
show the reaction diagram
(S)-perillyl alcohol + NAD+
(S)-perillaldehyde + NADH
show the reaction diagram
2,4-dihydroxy-3-(hydroxymethyl)-6-methylbenzoic acid + NAD+
3-formyl-2,4-dihydroxy-6-methylbenzoic acid + NADH
show the reaction diagram
2-aminobenzyl alcohol + NAD+
2-aminobenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
2-fluorobenzyl alcohol + NAD+
2-fluorobenzaldehyde + NADH
show the reaction diagram
2-hydroxybenzyl alcohol + NAD+
2-hydroxybenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
2-hydroxymethyl-6-methylnaphthalene + NAD+
2-formyl-6-methylnaphthalene + NADH
show the reaction diagram
2-hydroxymethylnaphthalene + NAD+
2-formylnaphthalene + NADH
show the reaction diagram
2-hydroxymethylthiophene + NAD+
2-formylthiophene + NADH
show the reaction diagram
2-methoxybenzyl alcohol + NAD+
2-methoxybenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
2-methylbenzyl alcohol + NAD+
2-methylbenzaldehyde + NADH
show the reaction diagram
3,4-dimethoxybenzyl alcohol + NAD+
3,4-dimethoxybenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
3,4-dimethylbenzyl alcohol + NAD+
3,4-dimethylbenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
3,5-dichlorobenzyl alcohol + NAD+
3,5-dichlorobenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
3-aminobenzyl alcohol + NAD+
3-aminobenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
3-chlorobenzyl alcohol + NAD+
3-chlorobenzaldehyde + NADH
show the reaction diagram
3-hydroxybenzyl alcohol + NAD+
3-hydroxybenzaldehyde + NADH
show the reaction diagram
3-methoxybenzyl alcohol + NAD+
3-methoxybenzaldehyde + NADH
show the reaction diagram
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
show the reaction diagram
3-methylbenzyl alcohol + NAD+
3-methylbenzaldehyde + NADH
show the reaction diagram
3-nitrobenzyl alcohol + NAD+
3-nitrobenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-aminobenzyl alcohol + NAD+
4-aminobenzaldehyde + NADH
show the reaction diagram
4-chlorobenzyl alcohol + NAD+
4-chlorobenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-ethylbenzyl alcohol + NAD+
4-ethylbenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-hydroxy-3-methoxybenzyl alcohol + NAD+
4-hydroxy-3-methoxybenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-hydroxybenzyl alcohol + NAD+
4-hydroxybenzaldehyde + NADH
show the reaction diagram
4-isopropylbenzyl alcohol + NAD+
4-isopropylbenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH
show the reaction diagram
-
-
-
-
r
4-methylbenzyl alcohol + NAD+
4-methylbenzaldehyde + NADH
show the reaction diagram
anisaldehyde + NADH + H+
anisic alcohol + NAD+
show the reaction diagram
-
relative activity: 72.2%
-
-
r
benzaldehyde + NAD(P)H + H+
benzyl alcohol + NAD(P)+
show the reaction diagram
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
show the reaction diagram
-
relative activity: 100%
-
-
r
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
show the reaction diagram
highest reductive activity with benzaldehyde
-
-
r
benzyl alcohol + NAD(P)+
benzaldehyde + NAD(P)H + H+
show the reaction diagram
benzyl alcohol + NAD+
benzaldehyde + NADH
show the reaction diagram
benzyl alcohol + NADP+
benzaldehyde + NADPH
show the reaction diagram
-
less active in the presence of NADP+ than in the presence of NAD+
-
-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
show the reaction diagram
-
-
-
r
cinnamaldehyde + NADH + H+
cinnamic alcohol + NAD+
show the reaction diagram
-
relative activity: 58.7%
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-
r
cinnamic aldehyde + NADH + H+
cinnamyl alcohol + NAD+
show the reaction diagram
cinnamyl alcohol + NAD(P)+
cinnamyl aldehyde + NAD(P)H + H+
show the reaction diagram
cinnamyl alcohol + NAD+
cinnamic aldehyde + NADH
show the reaction diagram
-
-
-
-
r
cinnamyl alcohol + NAD+
cinnamic aldehyde + NADH + H+
show the reaction diagram
cinnamyl alcohol + NAD+
cinnamyl aldehyde + NADH + H+
show the reaction diagram
-
67% of the activity with benzyl alcohol
-
-
?
cis-11-hexadecenal + NADH + H+
cis-11-hexadecenol + NAD+
show the reaction diagram
-
relative activity: 4.9%
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r
citral + NADH + H+
citryl alcohol + NAD+
show the reaction diagram
-
relative activity: 7.8%
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r
citronellal + NADH + H+
citronellol + NAD+
show the reaction diagram
-
relative activity: 21.8%
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r
coniferyl alcohol + NAD(P)+
coniferyl aldehyde + NAD(P)H + H+
show the reaction diagram
coniferyl alcohol + NAD+
coniferyl aldehyde + NADH + H+
show the reaction diagram
coniferyl aldehyde + NADH + H+
coniferyl alcohol + NAD+
show the reaction diagram
crotonaldehyde + NADPH + H+
crotonyl alcohol + NADP+
show the reaction diagram
-
-
-
r
crotonyl alcohol + NADP+
crotonaldehyde + NADPH + H+
show the reaction diagram
highest oxidative activity with crotyl alcohol
-
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r
decanal + NADH + H+
decanol + NAD+
show the reaction diagram
-
relative activity: 19.7%
-
-
r
dodecanal + NADH + H+
dodecanol + NAD+
show the reaction diagram
-
relative activity: 8.9%
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r
furan-2-methanol + NAD+
2-formylfuran + NADH
show the reaction diagram
-
-
-
-
r
furfuryl alcohol + NAD+
furfural + NADH
show the reaction diagram
geranial + NADH + H+
geraniol + NAD+
show the reaction diagram
-
-
-
-
r
geraniol + NAD(P)+
geranial + NAD(P)H + H+
show the reaction diagram
geraniol + NAD+
(2Z)-3,7-dimethylocta-2,6-dienal + NADH + H+
show the reaction diagram
-
105% of the activity with benzyl alcohol
-
-
?
geraniol + NAD+
geranial + NADH
show the reaction diagram
glutaraldehyde + NADH + H+
? + NAD+
show the reaction diagram
-
relative activity: 0.6%
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r
glyoxal + NADH + H+
? + NAD+
show the reaction diagram
-
relative activity: 0.7%
-
-
r
hexanal + NADH + H+
hexanol + NAD+
show the reaction diagram
-
relative activity: 6.4%
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-
r
hydroxybenzyl alcohol + NAD+
hydroxybenzaldehyde + NADH
show the reaction diagram
-
-
-
?
methoxybenzyl alcohol + NAD+
methoxybenzaldehyde + NADH
show the reaction diagram
-
-
-
?
methylbenzyl alcohol + NAD+
methylbenzaldehyde + NADH
show the reaction diagram
-
-
-
?
nerol + NAD(P)+
(2E)-3,7-dimethylocta-2,6-dienal + NAD(P)H + H+
show the reaction diagram
nerol + NAD+
(2E)-3,7-dimethylocta-2,6-dienal + NADH + H+
show the reaction diagram
-
116% of the activity with benzyl alcohol
-
-
?
nerol + NAD+
neral + NADH
show the reaction diagram
octanal + NADH + H+
octanol + NAD+
show the reaction diagram
-
relative activity: 36.5%
-
-
r
perillyl alcohol + NAD+
perillaldehyde + NADH
show the reaction diagram
-
-
-
-
r
phenethyl alcohol + NAD(P)+
phenylacetaldehyde + NAD(P)H + H+
show the reaction diagram
phenethyl alcohol + NAD+
phenylacetaldehyde + NADH + H+
show the reaction diagram
-
73% of the activity with benzyl alcohol
-
-
?
salicyl aldehyde + NADH + H+
salicyl alcohol + NAD+
show the reaction diagram
-
relative activity: 9%
-
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r
vanillin + NADH + H+
vanillin alcohol + NAD+
show the reaction diagram
-
relative activity: 4%
-
-
r
vanillyl alcohol + NAD+
vanillyl aldehyde + NADH + H+
show the reaction diagram
-
-
-
?
xylene-2,2'-diol + NAD+
? + NADH
show the reaction diagram
low activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,4-dihydroxy-3-(hydroxymethyl)-6-methylbenzoic acid + NAD+
3-formyl-2,4-dihydroxy-6-methylbenzoic acid + NADH
show the reaction diagram
-
the enzyme plays a role in the atranorin pathway
-
-
?
2-hydroxymethyl-6-methylnaphthalene + NAD+
2-formyl-6-methylnaphthalene + NADH
show the reaction diagram
2-hydroxymethylnaphthalene + NAD+
2-formylnaphthalene + NADH
show the reaction diagram
3-chlorobenzyl alcohol + NAD+
3-chlorobenzaldehyde + NADH
show the reaction diagram
benzaldehyde + NAD(P)H + H+
benzyl alcohol + NAD(P)+
show the reaction diagram
benzyl alcohol + NAD(P)+
benzaldehyde + NAD(P)H + H+
show the reaction diagram
benzyl alcohol + NAD+
benzaldehyde + NADH
show the reaction diagram
cinnamyl alcohol + NAD(P)+
cinnamyl aldehyde + NAD(P)H + H+
show the reaction diagram
coniferyl alcohol + NAD(P)+
coniferyl aldehyde + NAD(P)H + H+
show the reaction diagram
coniferyl alcohol + NAD+
coniferyl aldehyde + NADH + H+
show the reaction diagram
geraniol + NAD(P)+
geranial + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
hydroxybenzyl alcohol + NAD+
hydroxybenzaldehyde + NADH
show the reaction diagram
Q2Z1W3, Q2Z1W4, Q2Z1W5
-
-
-
?
methoxybenzyl alcohol + NAD+
methoxybenzaldehyde + NADH
show the reaction diagram
Q2Z1W3, Q2Z1W4, Q2Z1W5
-
-
-
?
methylbenzyl alcohol + NAD+
methylbenzaldehyde + NADH
show the reaction diagram
Q2Z1W3, Q2Z1W4, Q2Z1W5
-
-
-
?
nerol + NAD(P)+
(2E)-3,7-dimethylocta-2,6-dienal + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
phenethyl alcohol + NAD(P)+
phenylacetaldehyde + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
vanillyl alcohol + NAD+
vanillyl aldehyde + NADH + H+
show the reaction diagram
Q2Z1W3, Q2Z1W4, Q2Z1W5
-
-
-
?
xylene-2,2'-diol + NAD+
? + NADH
show the reaction diagram
Q2Z1W3, Q2Z1W4, Q2Z1W5
low activity
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
0.01 mM, residual activity: 0.2%
Cu2+
-
0.1 mM, residual activity: 1.3%
Fe2+
-
1 mM, residual activity: 21.7%
Hg+
-
0.001 mM, residual activity: 0.1%
Mn2+
-
1 mM, activity enhanced to 128%
Zn
-
zinc-dependent alcohol dehydrogenase. All of the residues involved in zinc binding are conserved
additional information
-
no effects on the enzyme activity by KCl, NaCl, and NiCl2, and by 10 mM urea and Tween-80
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2-Bromobenzaldehyde
-
0.01 mM, 88% inhibition
2-Chlorobenzaldehyde
-
0.01 mM, 95% inhibition
2-Fluorobenzaldehyde
-
0.1 mM, 100% inhibition
2-mercaptoethanol
3,4-dimethoxybenzaldehyde
-
0.1 mM, 10% inhibition
3-methylbenzaldehyde
-
0.1 mM, 75% inhibition
4-Isopropylbenzaldehyde
-
0.01 mM, 87% inhibition
5,5'-dithiobis-(2-nitrobenzoate)
-
-
AgNO3
dithiothreitol
-
above 2.5 mM
Fe3+
-
1 mM, 30% residual activity
iodoacetamide
iodoacetic acid
-
1 mM, 57% residual activity
N-bromosuccinimide
-
1 mM, 3% residual activity
N-ethylmaleimide
NADH
-
noncompetitive
p-chloromercuribenzoate
pentafluorobenzaldehyde
-
0.1 mM, 44% inhibition
SH-blocking agents
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
application of vanillin to the mycelium leads to up-regulation of enzymes involved in vanillin metabolism and also in glycolysis, the tricarboxylic acid cycle, the pentose-phosphate cycle, and heme biosynthesis, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
2-hydroxybenzyl alcohol
-
-
0.111
2-Methoxybenzyl alcohol
-
-
0.605 - 0.992
2-Methylbenzyl alcohol
0.053
3,4-dimethoxybenzyl alcohol
-
-
0.145
3-Methoxybenzyl alcohol
-
-
0.017 - 0.11
3-methyl-2-buten-1-ol
0.081 - 0.146
3-methylbenzyl alcohol
0.046 - 0.3
4-Hydroxybenzyl alcohol
0.111
4-Isopropylbenzyl alcohol
-
-
0.057
4-methoxybenzyl alcohol
-
-
0.106 - 0.118
4-methylbenzyl alcohol
0.0257 - 0.28
benzaldehyde
0.0173 - 0.32
benzyl alcohol
0.093 - 1.7
cinnamyl alcohol
0.044 - 0.28
coniferyl alcohol
5.1
coniferyl aldehyde
-
pH 8.0, 30°C
0.0152 - 0.4
NAD+
0.017 - 1.49
NADH
0.018
perillyl alcohol
-
-
0.111
thiophen-2-methanol
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
156
3-Methoxybenzyl alcohol
-
-
37 - 41
3-methyl-2-buten-1-ol
80
4-Hydroxybenzyl alcohol
-
-
144
4-Isopropylbenzyl alcohol
-
-
116
4-methoxybenzyl alcohol
-
-
622 - 12940
benzaldehyde
3.4 - 228
benzyl alcohol
116 - 141
cinnamyl alcohol
25.8 - 69.7
coniferyl alcohol
354
coniferyl aldehyde
-
pH 8.0, 30°C
53.7
NAD+
-
pH 8.0, 30°C
8920
NADH
-
pH 7.4, 30°C
83
perillyl alcohol
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
46700
benzaldehyde
-
pH 7.4, 30°C
68.3
cinnamyl alcohol
-
pH 8.0, 30°C
93.3 - 536
coniferyl alcohol
69.3
coniferyl aldehyde
-
pH 8.0, 30°C
134
NAD+
-
pH 8.0, 30°C
528000
NADH
-
pH 7.4, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
NADH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0002
-
biofilter culture cell extract, cofactor NADP+
0.016
-
liquid culture cell extract, cofactor NAD+
0.036
-
biofilter culture cell extract, cofactor NAD+
0.05
-
liquid culture cell extract, cofactor NADP+
0.106
-
-
0.22
-
recombinant strain
0.24
-
comparison to recombinant enzymes
10.7
-
puriifed recombinant enzyme, pH 8.5, 30°C
20.31 - 58.7
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
benzaldehyde + NADH
6
-
reduction of benzaldehyde
8
for crotonyl alcohol oxidation
8.9
-
benzaldehyde + NADH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6
-
pH 3.5: about 60% of maximal activity, pH 6.0: about 45% of maximal activity
4.7 - 7.6
-
less than half-maximal activity above and below, reduction of benzaldehyde
7.5 - 10.5
-
pH 7.5: about 15% of activity maximum, pH 10.5: about 20% of activity maximum
8.5 - 9.7
-
less than half-maximal activity above and below, oxidation of benzyl alcohol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
55
for crotonyl alcohol oxidation
65
for crotonaldehyde reduction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
20°C: about 60% of maximal activity, 50°C: about 70% of maximal activity
25 - 50
-
activity range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.04
-
sequence calculation
6.7
-
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
gel filtration
37598
-
4 * 37598, MALDI-TOF
38519
2 * 38519, sequence of cDNA
39500
-
SDS-PAGE
39700
-
4 * 39700, SDS-PAGE, cross-linking experiments in vitro using dimethylsuberimidate
42000
-
2 * 42000, SDS-PAGE
72600
-
gel filtration
75000
-
gel filtration, p-cresol grown cells
82000
-
gel filtration
90000
-
gel filtration
122000
-
gel filtration, 3,5-xylenol grown cells, activity 2
145000
-
gel filtration, 3,5-xylenol grown cells, activity 1
150000
-
recombinant enzyme, gel filtration
151000
-
gel filtration
155000
-
gel filtration
160000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
-
-
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
-
75 h, more than 80% of initial activity
724592
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
enzyme reaches 52% of its maximum activity at 15°C
30 - 50
-
the purified recombinant enzyme remains quite stable
37
-
after 21 h no loss of activity
50
-
pH 7.0, stable up to
55
the enzyme shows moderate thermostability with a half-life of 6.2 h at 55°C
56
-
after 10 min complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
benzyl alcohol stabilizes slightly
-
dithiothreitol stabilizes
-
MgCl2 stabilizes slightly
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DMSO
the enzyme retains 87.5% of the initial activity after 24 h of incubation with 20% (v/v) dimethyl sulfoxide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, concentrated, mixed with ethanediol
-
-70°C, enzyme dialyzed against buffer containing 40% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme also capable of oxidizing aliphatic primary alcohols with NAD+
-
enzyme encoded by plasmid TOL
-
ion-exchange chromatography, hydrophobic interaction chromatography, ultrafiltration, affinity chromatography
-
partially, subcellular fractionation
-
recombinant enzyme about 40fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, hydrophobic interaction chromatography, again dialysis, and anion exchange chromatography
-
recombinant lp_3054 from Escherichia coli strain JM109
-
two distinct NAD+-dependent m-hydroxybenzyl alcohol dehydrogenases from cells grown on 3,5-xylenol, differing in relative rates with the various substrates, another NAD+-dependent alcohol dehydrogenase, not identical with the former ones from p-cresol-grown cells
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant enzyme overexpression in Escherichia coli strain BL21(DE3), optimization of conditions and method for soluble CADH expression, expression of active CADH under optimized conditions is approximately 4fold higher than in the absence of heat shock, solution of inclusion body formation by heat-shock treatment of recombinant Escherichia coli carrying the Streptomyces CADH gene
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expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli XL1-Blue
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gene adhA, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression in Escherichia coli; gene adhB, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression in Escherichia coli; gene adhC, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression in Escherichia coli
gene lp_3054, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H47Q
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increased Km for benzyl alcohol and benzaldehyde, decreased Km for NAD+ and NADH
H47Q/V61H
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unchanged Km for benzyl alcohol, decreased Km for NAD+ and benzaldehyde
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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biotechnological production of vanillin
degradation
synthesis
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biotechnological production of vanillin
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