Information on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.195
-
RECOMMENDED NAME
GeneOntology No.
cinnamyl-alcohol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
capsiconiate biosynthesis
-
-
phenylpropanoid biosynthesis
Phenylpropanoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
cinnamyl-alcohol:NADP+ oxidoreductase
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
CAS REGISTRY NUMBER
COMMENTARY hide
55467-36-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Abies nobilis
-
-
-
Manually annotated by BRENDA team
A3 and A6
-
-
Manually annotated by BRENDA team
M20 and M22
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Corylus sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Eucalyptus sp.
-
-
-
Manually annotated by BRENDA team
gene Fxcad1; cv. Chandler, octaploid cultivar, gene Fxcad1 and Fxcad2
SwissProt
Manually annotated by BRENDA team
var. Mandarin
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
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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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene Gold-hull-and-internode2, i.e. gene GH2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Japanese black pine
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Platanus x acerifolia
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pteris wimsetti
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
Sphagnum sp.
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain PCC 6803
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
neoformed calli induced by Agrobacterium rhizogenes on Phaseolus mungo hypocotyl
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-
Manually annotated by BRENDA team
cv. Canary Bird
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
2,4-dimethylcinnamyl alcohol + NADP+
2,4-dimethylcinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
2-propanol + NADP+
? + NADPH + H+
show the reaction diagram
-
2-propanol can be also used in the cofactor recycling catalytic system as co-solvent like ethanol, but at the same time cinnamaldehyde conversion is lower (85%) and cinnamyl alcohol production is accordingly lower
-
-
-
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
show the reaction diagram
3,4-methylenedioxycinnamyl alcohol + NADP+
3,4-methylenedioxycinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
3-methoxybenzylalcohol + NADP+
3-methoxybenzaldehyde + NADPH
show the reaction diagram
-
-
-
-
3-phenyl-1-propanol + NAD+
3-phenylpropanal + NADH + H+
show the reaction diagram
4-bromocinnamyl alcohol + NADP+
4-bromocinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
4-chlorocinnamyl alcohol + NADP+
4-chlorocinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
4-coumaraldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
show the reaction diagram
-
-
-
?
4-methoxybenzylalcohol + NADP+
4-methoxybenzaldehyde + NADPH
show the reaction diagram
-
-
-
-
4-methoxycinnamyl alcohol + NADP+
4-methoxycinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
4-methylcinnamyl alcohol + NADP+
4-methylcinnamaldehyde + NADPH
show the reaction diagram
-
-
-
-
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
show the reaction diagram
-
-
-
r
5-hydroxyconiferyl aldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
show the reaction diagram
-
-
-
r
allyl alcohol + NAD+
prop-2-enal + NADH + H+
show the reaction diagram
benzaldehyde + NADP+
benzoic acid + NADPH
show the reaction diagram
-
the enzyme also shows dismutase activity
-
-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH
show the reaction diagram
-
-
-
-
r
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
show the reaction diagram
CAD4 displays slight activity for benzoyl alcohol
-
-
?
benzyl alcohol + NADP+
benzylaldehyde + NADPH + H+
show the reaction diagram
slight activity
-
-
r
benzylalcohol + NADP+
benzaldehyde + NADPH
show the reaction diagram
-
-
-
-
butanol + NADP+
butyraldehyde + NADPH
show the reaction diagram
-
-
-
-
r
caffeoyl aldehyde + NADPH + H+
caffeoyl alcohol + NADP+
show the reaction diagram
-
-
-
r
caffeyl aldehyde + NADPH
caffeyl alcohol + NADP+
show the reaction diagram
-
-
-
r
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
show the reaction diagram
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
show the reaction diagram
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
show the reaction diagram
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
show the reaction diagram
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
show the reaction diagram
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH + H+
show the reaction diagram
-
-
-
?
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
show the reaction diagram
-
-
-
r
coniferol + NADP+
coniferyl aldehyde + NADPH
show the reaction diagram
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
show the reaction diagram
coniferyl alcohol and NADP+
coniferyl aldehyde + NADPH + H+
show the reaction diagram
-
-
-
-
?
coniferyl aldehyde + NADPH
coniferol + NADP+
show the reaction diagram
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
show the reaction diagram
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
show the reaction diagram
coumaryl alcohol + NADP+
coumaraldehyde + NADPH + H+
show the reaction diagram
-
-
-
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
show the reaction diagram
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
show the reaction diagram
-
-
-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
show the reaction diagram
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
show the reaction diagram
-
-
-
r
propanol + NADP+
propionaldehyde + NADPH
show the reaction diagram
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
show the reaction diagram
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
show the reaction diagram
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
show the reaction diagram
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
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
show the reaction diagram
-
-
-
-
r
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
show the reaction diagram
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
show the reaction diagram
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
show the reaction diagram
O49482, P48523
-
-
-
r
coniferol + NADP+
coniferyl aldehyde + NADPH
show the reaction diagram
Q02971
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
show the reaction diagram
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
show the reaction diagram
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
show the reaction diagram
Q02971
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
NADPH is about 4000fold less effective than NADH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 2',5'-diphosphate
-
-
adenosine 5'-monophosphate
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
benzyl alcohol
-
competitive mechanism, substrate inhibition
cinnamaldehyde
-
substrate inhibition mediated by cinnamaldehyde concentrations far from the Km value of 0.46 mM, which does not allow for excessively increasing the starting cinnamaldehyde concentration, since the process yield may be greatly affected
cinnamyl alcohol
-
competitive mechanism, substrate inhibition
coniferin
-
with coniferyl alcohol as substrates, noncompetitive inhibition
coniferyl alcohol
-
competitive mechanism, substrate inhibition
Fe3+
-
1 mM, 74% residual activity
flavones
Eucalyptus sp.
-
IC50: 0.07-0.055 mM
iodoacetic acid
-
1 mM, 56% residual activity
N-bromosuccimide
-
1 mM, 56% residual activity
Ni
-
CAD activity is not affected by concentrations up to 0.12 mM, phenolic metabolism is not substantially affected by Ni excess
RNAi
-
RNAi-mediated transient gene silencing in the epidermis leads to a higher penetration efficiency of Blumeria graminis f. sp. tritici (64%) than in the controls. Gene silencing also compromises penetration resistance to varying degrees with different genes against an inappropriate pathogen, Blumeria graminis f. sp. hordei. Co-silencing of CAD and other genes involved in monolignol biosynthesis leads to greater penetration of Blumeria graminis f. sp. tritici or Blumeria graminis f. sp. hordei than when the genes are silenced separately. Gene silencing hamperes host autofluorescence response at fungal contact sites
-
Zn2+
-
1 mM, 80% residual activity
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO2
-
high CO2 stimulates progressively the enzyme, as well as of other enzymes involved in metabolism of phenolic compounds, overview
jasmonate
accumulation of CAD mRNA in response to jasmonate application and mechanical wounding
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036
3,4-dimethoxy-cinnamyl alcohol
-
-
0.0069 - 0.043
3,4-dimethoxycinnamaldehyde
0.022
3,4-dimethoxycinnamyl alcohol
-
-
0.106
3-Methoxybenzaldehyde
-
-
0.96
3-Phenyl-1-propanol
-
pH 8.0, 30C
0.013 - 0.117
4-coumaraldehyde
0.13
4-methoxybenzaldehyde
-
-
0.034
4-methoxycinnamyl alcohol
-
-
0.0244
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.04
acetaldehyde
-
pH 7.5, 37C, recombinant enzyme
0.5
allyl alcohol
-
pH 8.0, 30C
0.03 - 31
benzaldehyde
0.41 - 2.6
benzyl alcohol
9
butanol
-
pH 7.5, 37C, recombinant enzyme
0.0891
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0025 - 0.92
cinnamaldehyde
0.0122 - 0.27
cinnamyl alcohol
0.005
cinnamyl aldehyde
-
pH 7.5, 37C, recombinant enzyme
0.00077 - 0.012
coniferaldehyde
0.00098 - 0.677
coniferyl alcohol
0.0018 - 0.053
coniferyl aldehyde
0.0042
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
46
ethanol
-
pH 7.5, 37C, recombinant enzyme
0.052 - 1.23
NAD+
0.016 - 0.071
NADH
0.0038 - 0.06
NADP+
0.0046 - 0.15
NADPH
0.0012 - 0.03
p-coumaraldehyde
0.034 - 0.283
p-coumaryl alcohol
0.0272
p-coumaryl aldehyde
pH not specified in the publication, temperature not specified in the publication
13
Propanol
-
pH 7.5, 37C, recombinant enzyme
0.0043 - 0.147
sinapaldehyde
0.0156 - 0.56
sinapyl alcohol
0.005 - 0.0406
sinapyl aldehyde
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.2
3-Phenyl-1-propanol
Streptomyces sp.
-
pH 8.0, 30C
0.026 - 74.2
4-coumaraldehyde
16.7
acetaldehyde
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
32.9
allyl alcohol
Streptomyces sp.
-
pH 8.0, 30C
2.3 - 2.5
benzaldehyde
8.4
benzyl alcohol
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
5.7
butanol
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
14.4 - 107.9
cinnamaldehyde
13.3 - 60.78
cinnamyl alcohol
7.7
cinnamyl aldehyde
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
0.43 - 13.2
coniferyl alcohol
0.17 - 138
coniferyl aldehyde
24.7
coumaryl alcohol
Panicum virgatum
E2DIF4, E2DIF5
pH not specified in the publication, temperature not specified in the publication
7.1
ethanol
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
0.0242 - 33
NAD+
43
NADH
Geobacillus stearothermophilus
-
pH 7.5, 50C
0.0555 - 15.5
NADP+
0.49 - 25.2
NADPH
12.8
Propanol
Helicobacter pylori
-
pH 7.5, 37C, recombinant enzyme
46.4
sinapyl alcohol
Panicum virgatum
E2DIF4, E2DIF5
pH not specified in the publication, temperature not specified in the publication
3.4 - 196
sinapyl aldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.6
3-Phenyl-1-propanol
Streptomyces sp.
-
pH 8.0, 30C
5108
0.23 - 2061
4-coumaraldehyde
6121
0.169
5-hydroxyconiferyl aldehyde
Triticum aestivum
D7PGW0
pH not specified in the publication, temperature not specified in the publication
14005
66.5
allyl alcohol
Streptomyces sp.
-
pH 8.0, 30C
3612
0.082
caffeoyl aldehyde
Triticum aestivum
D7PGW0
pH not specified in the publication, temperature not specified in the publication
5329
15.6 - 1835
cinnamaldehyde
1071
106 - 391
cinnamyl alcohol
936
13400
coniferyl alcohol
Panicum virgatum
E2DIF4, E2DIF5
pH not specified in the publication, temperature not specified in the publication
1202
0.896 - 35800
coniferyl aldehyde
1677
5880
coumaryl alcohol
Panicum virgatum
E2DIF4, E2DIF5
pH not specified in the publication, temperature not specified in the publication
12482
73 - 387
NAD+
7
2687
NADH
Geobacillus stearothermophilus
-
pH 7.5, 50C
8
0.25
p-coumaryl aldehyde
Triticum aestivum
D7PGW0
pH not specified in the publication, temperature not specified in the publication
84014
2980
sinapyl alcohol
Panicum virgatum
E2DIF4, E2DIF5
pH not specified in the publication, temperature not specified in the publication
3670
0.286 - 20500
sinapyl aldehyde
5313
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.45
adenosine 2',5'-diphosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.58
adenosine 5'-monophosphate
Eucalyptus gunnii
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
0.07 - 0.055
flavones
Eucalyptus sp.
-
IC50: 0.07-0.055 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00007
-
crude extract from young etiolated shoots
0.00125
-
induced cell culture
0.0014
-
substrate coniferyl aldehyde, recombinant enzyme encoded by GH2
0.0034
-
crude extract from bean pods
0.0036
-
substrate sinapyl aldehyde, recombinant enzyme encoded by GH2
0.006
-
elicitor-treated wheat leaves
0.18
-
crude extract from differentiating xylem
0.33
-
recombinant enzyme, with NAD+ as cofactor
0.39
-
S212D mutant, with NAD+ as cofactor
1.67
-
S212D mutant, with NADP+ as cofactor
3.86
-
-
4.7
-
recombinant enzyme, with NADP+ as cofactor
56.4
-
-
64.56
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.25
assay at, forward reaction; assay at, forward reaction
7.5
-
assay at
9
-
coniferyl alcohol oxidation dependent on ionic strength
10.5
reverse reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
-
pH 4.5: about 55% of activity maximum, pH 8.5: about 30% of activity maximum
6 - 8
-
coniferyl aldehyde reduction, pH 6.0: about 70% of activity maximum, pH 8.0: about 30% of activity maximum
7.2 - 9.7
-
coniferyl alcohol oxidation, pH 7.2: about 40% of activity maximum, pH 9.7: about 35% of activity maximum
8
more than 70% of the maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
about 85% loss of initial activity
60
complete loss of activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
calculated
5.8
calculated
6.3
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
shell zone, immunogold-electron microscopy of shoot apex
Manually annotated by BRENDA team
-
CAD is accumulated in the epidermis, CAD gene expression after pathogen attack is predominantly in the epidermis
Manually annotated by BRENDA team
expression in all fruit ripening stages
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
expression of isoforms Cad-2, Cad-3
Manually annotated by BRENDA team
-
all CAD genes expressed, but at different levels
Manually annotated by BRENDA team
-
immunogold-electron microscopy of shoot apex
Manually annotated by BRENDA team
-
developing, immunogold-electron microscopy of shoot apex
Manually annotated by BRENDA team
-
immunogold-electron microscopy of mature stems
Manually annotated by BRENDA team
-
developing
Manually annotated by BRENDA team
-
immunogold-electron microscopy of shoot apex
Manually annotated by BRENDA team
-
differentiating element
Manually annotated by BRENDA team
-
predominant expression of isoforms Cad-1, Cad-9
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
14 of the 15 CAD genes are distributed on duplicated regions
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
SDS-PAGE, isoform CAD1
35790
-
calculated from cDNA sequence
38570
-
calculated from cDNA sequence
39000
-
Western blotting analysis
43000
-
Western blot analysis
45000
-
SDS-PAGE
69000
-
gel filtration
70000
-
gel filtration
72000
-
gel filtration (with Superose 12)
82000
-
gel filtration (on Sephacryl 200)
143000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant isozyme CAD5, 4-10 mg/ml apo-protein in 20 mM Tris-HCl, pH 8.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, at 4C or at 20C, 2fold dilution with reservoir solution containing 20% w/v PEG 3350, and 0.2 M trilithium citrate tetrahydrate, pH 8.1 3 days, X-ray diffraction structure determination an analysis at 2.0-2.6 A resolution
in complex with NADP(H), to 2.18 A resolution. NADP(H) is bound through hydrophobic interactions within the well-conserved GXGGXG motif from residues Gly184 to Gly189 and the adenine ring is the syn-conformation and is sandwiched between the guanidino group of Arg208 and Thr244 side chains. The aromatic side chains of residues Phe114 and Tyr116 in the active site could bind aromatic aldehydes by stacking the aromatic head of the substrates
homology modeling based on structure of Arabidopsis thaliana isoform CAD5. The model reveals a trilobed structure. The two major lobes contribute to constitution of NADP+ binding, catalytic Zn2+ binding and substrate binding domains. The substrate binding pocket is protected by these two major lobes and is in close proximity of catalytic Zn2+ and NADP+ binding domains
10 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml of both protein and reservoir solution, the latter containing 1. 1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, or 2.30% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, room temperature, about 1 week, trigonal or monoclinic crystals, X-ray diffraction structure determination and analysis at 3.1 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
-
75 h, more than 80% of initial activity
724592
6.8 - 8.4
-
maximum stability
347811
6.8
-
unstable below
347811
7
-
no significant activity loss up to 24 h
696846
7.5
-
4C, 1 week, 50% loss of activity
288228
9
almost complete loss of activity
712611
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
up to 30C, retains all initial catalytic activity, only 18% activity is lost at 40C, at 60C 100% loss of activity
40
-
rapid inactivation above
50
-
pH 7.0, stable up to
60
complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
2-mercaptoethanol: stable in presence of high concentration
-
60% loss of activity after 20 h incubation in buffer containing a divalent cation-exchange resin
-
dithiothreitol stabilizes
-
ethylene glycol stabilizes
-
ethylene glycol stabilizes dilute solutions
-
freezing of glycerol containing fractions causes 50% loss of activity after 24 h
-
glycerol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 20 or 50% glycerol, several months
-
-20C, 42 mM 2-mercaptoethanol, 10% ethylene glycol, 5 months
-
-20C, NADP+, mercaptoethanol, ethylene glycol, several months
-
-20C, purified recombinant His-tagged enzyme, 75 mM sodium phosphate, pH 7.5, 5 mM DTT, no loss of activity after 1 month
-
4C, mercaptoethanol, ethylene glycol, 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity purification on a nickel column; by affinity purification on a nickel column; recombinant enzyme; recombinant enzyme
recombinant enzyme from strain BL9 by DEAE ion exchange, Red-Sepharose, and gel filtration chromatography
-
recombinant GH2-encoded CAD from Escherichia coli
-
recombinant GST-fusion enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography; recombinant GST-fusion enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant isozyme CAD4 from Escherichia coli; recombinant isozyme CAD5 from Escherichia coli
two isoforms
-
var. Mandarin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.3 kb cDNA fragment cloned into pGEM-T Easy vector and transformed into competent cell of DH5alpha from Escherichia coli
9 AtCAD genes, 2 paralogs AtCAD-C and AtCAD-D, DNA and amino acid sequence determination and analysis, tissue expression pattern study of wild-type and mutant plants
construct pCFC1 containing the entire 8.8 kb open reading frame, 3253 bp upstream sequences, and the 1646 bp downstream region and an empty pCAMBIA2301 vector introduced into the fc1 mutant by Agrobacterium tumefaciens-mediated transformation
entire coding regions of CAD4 cloned into the pET30a vector and expressed in Escherichia coli Rossetta R2 cells; entire coding regions of CAD4 cloned into the pET30a vector and expressed in Escherichia coli Rossetta R2 cells; expression in Escherichia coli; expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
from an expression sequence tag (EST) library, amplified fragments ligated into TOPO cloning vector. EST fragments in an entry vector cloned into the RNAi destination vector pIPKTA30N
-
gene CAD or HP1140 from strain 26995, cloning in Escherichia coli strain DH5alpha, and expression in strain BL21(DE3) as N-terminally His-tagged enzyme
-
gene CAD, DNA and amino acid sequence determination of several CAD isozyme genes, expression analysis in wild-type and cad-c-cad-d-double mutant cells, overview
gene CAD, genetic organization, DNA and amino acid sequence determination
-
gene CAD1, DNA and amino acid sequence determination and analysis, phylogenetic tree of the CAD protein family, quantitative expression analysis, expression in Escherichia coli, complementation of the cad-c-cad-d-double mutant with different CAD genes has different effects on lignin monomer synthesis, overview
gene CAD1-1, DNA and amino acid sequence determination and analysis, expression analysis, recombinant expression as GST-fusion enzyme in Escherichia coli strain BL21; gene CAD1-7, DNA and amino acid sequence determination and analysis, expression analysis, recombinant expression as GST-fusion enzyme in Escherichia coli strain BL21
gene Gold-hull-and-internode2, i.e. gene GH2, DNA and amino acid sequence determination and analysis, map-based cloning approach, phylogenetic and expression pattern analysis, expression of GH2 in Escherichia coli
-
genes Fxcad1 and Fxcad2, DNA and amino acid sequence determination and analysis, expression of gene Fxcad1 in Escherichia coli and in Pichia pastoris, in the latter case as an extracellular protein
genomic fragment giving the CAD promoter (829 bp) amplified
-
isozyme CAD4, expression in Escherichia coli; isozyme CAD5, expression in Escherichia coli
overexpression in strain BL9
-
partial DNA and amino acid sequence determination and analysis
Picea glauca seedlings line Pg653 stably transformed with a DNA fragment of 1163 base pairs (CAD) fused to the beta-glucuronidase gene
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of isoform CAD3 is strongly up-regulated in tea plants after Ectropic oblique attack and mechanical damage. Presence of abscisic acid induces isoform CAD3 expression; methyl jasmonate and salicylic acid elevate the expression of isoform CAD1; methyl jasmonate and salicylic acid elevate the expression of isoform CAD2
gene transcripts are highly induced by cold, wounding, and reactive oxygen species. Promoter activity is strongly induced in response to the biotic and abiotic stresses, with the strongest inducer being wounding, and is also induced by salicylic acid and jasmonic acid as well as by abscisic acid and 6-benzylaminopurine
inoculation of sugarcane stems with Sporisorium scitamineum elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
mRNA is highly expressed in stems at the elongation and heading stages. At the milky stage of wheat, CAD1 mRNA abundance, protein level and enzyme activity in stem tissues are higher in lodging-resistant cultivar H4546 than in lodging-sensitive cultivar C6001
presence of abscisic acid does not induce isoform CAD2 expression
presence of Zn2+ is essential for the expression of enzyme, as no expression is observed in absence of Zn2+
treatment of seedling with exogenous abscisic acid, salicylic acid, ethephon, ultraviolet and wounding leads to increase in expression