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Information on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase
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1.1.1.195 cinnamyl-alcohol dehydrogenaseIUBMB Comments
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
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Word Map
- 1.1.1.195
- lignin
-
lignification
-
monolignols
-
phenylpropanoids
-
sinapyl
-
ammonia-lyase
-
coniferyl
- xylem
- coniferaldehyde
- cinnamoyl-coa
-
caffeic
-
guaiacyl
- sinapaldehyde
- eucalyptus
-
syringyl
-
p-coumaryl
-
linum
- podophyllotoxin
- taeda
-
cinnamoyl
-
loblolly
- gunnii
- agriculture
- cinnamaldehydes
-
hydroxycinnamyl
-
4-coumarate-coa
- synthesis
- 4-coumarate
- syringaldehyde
-
3-o-methyltransferase
- nutrition
-
cadherin-11
-
thioacidolysis
-
4.3.1.5
- biofuel production
- industry
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ADH, AdhA, alcohol dehydrogenase, AtCAD4, BdCAD1, Bmr6, Bradi3g06480, brown midrib6, Brown-midrib 1 protein, CAD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BdCAD1
Brown-midrib 1 protein
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CAD
CAD 7/8
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-
-
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CAD1
CAD12
CAD2
CAD3
CAD4
CAD5
CAD6
CAD7
CAD8
CAD9
cinnamyl alcohol dehydrogenase
cinnamyl alcohol dehydrogenase 1
cinnamyl alcohol dehydrogenase 2
dehydrogenase, cinnamyl alcohol
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-
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CAD
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-
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CAD
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CAD2
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-
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cinnamyl alcohol dehydrogenase
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-
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cinnamyl alcohol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
A-specific enzyme
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
A-specific enzyme; ordered bi-bi mechanism
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
acts stereospecifically on the pro-R-hydrogen atom of coniferyl alcohol
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
active site structure
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
catalytic reaction mechanism, substrate and cofactor binding structure; catalytic reaction mechanism, substrate and cofactor binding structure
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
random mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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CAS REGISTRY NUMBER
COMMENTARY
55467-36-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dimethylcinnamyl alcohol + NADP+
2,4-dimethylcinnamaldehyde + NADPH
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-
-
-
2-propanol + NADP+
? + NADPH + H+
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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
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-
3,4-methylenedioxycinnamyl alcohol + NADP+
3,4-methylenedioxycinnamaldehyde + NADPH
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-
-
-
3-methoxybenzylalcohol + NADP+
3-methoxybenzaldehyde + NADPH
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-
-
-
4-bromocinnamyl alcohol + NADP+
4-bromocinnamaldehyde + NADPH
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-
-
-
4-chlorocinnamyl alcohol + NADP+
4-chlorocinnamaldehyde + NADPH
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-
-
-
4-methoxybenzylalcohol + NADP+
4-methoxybenzaldehyde + NADPH
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-
-
-
4-methoxycinnamyl alcohol + NADP+
4-methoxycinnamaldehyde + NADPH
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-
-
-
4-methylcinnamyl alcohol + NADP+
4-methylcinnamaldehyde + NADPH
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-
-
-
5-hydroxyconiferyl aldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
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-
?
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
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-
-
r
5-hydroxyconiferyl aldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
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-
-
r
5-hydroxyconiferylaldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
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-
?
5-hydroxyconiferylaldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
lowest catalytic efficiency
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?
benzaldehyde + NADP+
benzoic acid + NADPH
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the enzyme also shows dismutase activity
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-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
CAD4 displays slight activity for benzoyl alcohol
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-
?
benzyl alcohol + NADP+
benzylaldehyde + NADPH + H+
slight activity
-
-
r
caffeylaldehyde + NADP+
caffeyl alcohol + NADPH + H+
low activity
-
-
?
caffeylaldehyde + NADPH + H+
caffeyl alcohol + NADP+
-
-
-
?
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
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-
-
r
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
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-
-
r
p-coumarylaldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
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-
-
?
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
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-
-
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-
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
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-
-
r
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
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-
-
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-
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
catalytic preference for 4-coumaraldehyde
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?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
high catalytic efficiency
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?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
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cofactor recycling catalytic system in which ADH reduces cinnamaldehyde to cinnamyl alcohol (oxidizing NADH to NAD+). THe NAD+ produced is then recycled by ADH at expense of ethanol, which acts as co-solvent for both substrate and product, and is present in large excess to force the whole process toward cinnamaldehyde reduction. Also, elimination of the obtained dehydrogenation product acetaldehyde drives cinnamaldehyde reduction toward completion. 1-2 mM is the ideal starting cinnamaldehyde concentration
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?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
key enzyme in lignin biosynthesis
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?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
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involved in lignin biosynthesis
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?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
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r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
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-
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
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100% activity with 1 mM cinnamyl alcohol, 116% activity with 10 mM cinnamyl alcohol, reaction catalyzed by unspecific alcohol dehydrogenase (EC 1.1.1.1)
61% activity with 0.1 mM cinnamaldehyde, 7% activity with 1 mM cinnamaldehyde
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r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
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the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
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?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
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?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
favourite substrate
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?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
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isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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-
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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-
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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-
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4. Activity of Bmr6 is 2.5- and 34fold higher than CAD4 for coniferyl and sinapyl aldehyde, respectively
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4. Bmr6 activity is 2.2- and 2.6-fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates. Activity of Bmr6 is 2.5- and 34fold higher than CAD4 for coniferyl and sinapyl aldehyde, respectively
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
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r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
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r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
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recombinant enzyme encoded by gene GH2
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
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-
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
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the forward reaction is the physiological reaction
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
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-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
low activity
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
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r
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
-
-
-
r
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4
-
-
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
?
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
preferred substrate
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
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recombinant enzyme encoded by gene GH2
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
low activity
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?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
very low activity
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
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-
r
additional information
?
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32 single nucleotide polymorphisms in the coding region of CAD, whereby 12 are nonsynonymous mutations and 20 are synonymous mutations. 11 and three synonymous mutations are detected in Acacia auriculiformis A3 x Acacia mangium M22 and Acacia auriculiformis A6 x Acacia mangium M20 parental combination, respectively. The synonymous mutations detected are 20 in both genes. The high occurences of single nucleotide polymorphisms are possible because the plant has to adopt physiologically to a variety of unpredictable environmental conditions
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additional information
?
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32 single nucleotide polymorphisms in the coding region of CAD, whereby 12 are nonsynonymous mutations and 20 are synonymous mutations. 11 and three synonymous mutations are detected in Acacia auriculiformis A3 x Acacia mangium M22 and Acacia auriculiformis A6 x Acacia mangium M20 parental combination, respectively. The synonymous mutations detected are 20 in both genes. The high occurences of single nucleotide polymorphisms are possible because the plant has to adopt physiologically to a variety of unpredictable environmental conditions
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additional information
?
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role of the enzyme in lignin biosynthesis and structure formation
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additional information
?
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the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
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additional information
?
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substrate specificity of isozyme CAD4
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additional information
?
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substrate specificity of isozyme CAD4
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additional information
?
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substrate specificity of isozyme CAD5
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additional information
?
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substrate specificity of isozyme CAD5
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additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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-
additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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additional information
?
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substituted and unsubstituted benzaldehydes
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additional information
?
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enzyme involved in lignification in vascular plants
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additional information
?
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not: methanol, ethanol, n-propanol, n-butanol, isobutanol, geraniol, various aromatic alcohols (e.g. salicyl alcohol, vanillyl alcohol, piperonyl alcohol)
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-
additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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additional information
?
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coniferylaldehyde and sinapylaldehyde are the preferred substrates
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-
additional information
?
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coniferylaldehyde and sinapylaldehyde are the preferred substrates
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additional information
?
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no activity with methanol and ethanol as alcoholic substrates
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additional information
?
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the enzyme shows broad substrate specificity, LlCAD2 shows significant activity against cinnamyl substrates, but is almost inactive against aliphatic and other benzyl compounds. Possible involvement of histidine at the active site. Low activity with benzaldehyde, anisaldehyde, vanillin, and syringaldehyde. No or very poor activity with formaldehyde, acetaldehyde, propionaldehyde, and butryaldehyde
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additional information
?
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the enzyme shows broad substrate specificity, LlCAD2 shows significant activity against cinnamyl substrates, but is almost inactive against aliphatic and other benzyl compounds. Possible involvement of histidine at the active site. Low activity with benzaldehyde, anisaldehyde, vanillin, and syringaldehyde. No or very poor activity with formaldehyde, acetaldehyde, propionaldehyde, and butryaldehyde
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additional information
?
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the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
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additional information
?
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the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
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additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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additional information
?
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the enzyme Mt-CAD2 shows low activity with all substrates and compared to the activities of Mt-CAD1, substrate binding and specificity of Mt-CAD2, overview
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additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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additional information
?
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FC1 plays an important role in the biosynthesis of lignin and the control of culm strength in rice, especially in the first internodes, and FC1 deficiency in the first internodes is the main cause of the lodging trait in fc1 plants. FC1 mutant exhibits an abnormal development phenotype, including late heading time, semi-dwarf habit, and causes a reduction in cell wall thickness, as well as a decrease in lignin. Extracts from the first internodes and panicles of FC1 plants exhibit drastically reduced cinnamyl-alcohol dehydrogenase activity. Overexpression of FC1 does not affect the cell wall composition
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additional information
?
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not: sinapaldehyde, 4-hydroxybenzaldehyde, vanillin, 4-hydroxy-3,5-dimethoxybenzaldehyde, 3,4-dimethoxybenzaldehyde, salicylaldehyde, 2-methoxybenzaldehyde, mannose, acetaldehyde
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additional information
?
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final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
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additional information
?
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beta-glucuronidase expression driven by the CAD promoter is wound-inducible
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additional information
?
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beta-glucuronidase expression driven by the CAD promoter is wound-inducible
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additional information
?
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liginification and lignin topochemistry indifferent samples, overview
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additional information
?
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the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
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additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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-
additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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KJ159967
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
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additional information
?
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CAD4 and CAD10 possess transcription factor binding motifs involved in development and in response to various stresses. CAD1, CAD2, CAD10, and CAD11 possess promoter motifs involved in the response to fungal elicitors. CAD2, CAD4, CAD5, CAD7, CAD9, rCAD10 and CAD16 possess motifs involved in response to wounding, herbivore stress, as well as other stresses
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additional information
?
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one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
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-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
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-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
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-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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-
-
additional information
?
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a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
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-
additional information
?
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a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
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additional information
?
-
-
a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
-
-
-
additional information
?
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
-
CAD is one of the enzymes involved in monolignol biosynthesis, which is critically important for host defence against both appropriate and inappropriate pathogen invasion in wheat
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
key enzyme in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
involved in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
the forward reaction is the physiological reaction
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
low activity
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
very low activity
-
-
r
additional information
?
-
role of the enzyme in lignin biosynthesis and structure formation
-
-
-
additional information
?
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
enzyme involved in lignification in vascular plants
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
-
-
-
additional information
?
-
-
liginification and lignin topochemistry indifferent samples, overview
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
cofactor binding site structure determination and analysis; cofactor binding site structure determination and analysis
NADP+
-
NADPH
-
dependent for, binding and specificity mechanism, interaction through Ser210, Arg211, and Lys215 and the terminal phosphate group
NADPH
cofactor binding site structure determination and analysis; cofactor binding site structure determination and analysis
NADPH
the NADPH binding sequence is located at amino acid residues 188-193; the NADPH binding sequence is located at amino acid residues 189-194; the NADPH binding sequence is located at amino acid residues 191-196
NADPH
; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling
additional information
the enzyme has a highly conserved Rossmann fold NAD(P)H/NAD(P)+ binding domain
-
additional information
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
additional information
-
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
additional information
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
additional information
-
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
-
activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+
EDTA
-
activates at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
additional information
Zn2+
ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70; zinc-type enzyme, ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
required, the enzyme contains the Zn-1 binding domain motif GHE(X)2G(X)5G(X)2V and the conserved Zn-1 catalytic residues C47, H69, and C163
Zn2+
required, Zn1 binding sequence is located at amino acid residues 68-82, and Zn2 binding sequence is located at amino acid residues 88-113; required, Zn1 binding sequence is located at amino acid residues 69-83, and Zn2 binding sequence is located at amino acid residues 89-114; required, Zn1 binding sequence is located at amino acid residues 71-85, and Zn2 binding sequence is located at amino acid residues 91-116
Zn2+
required; required, Zn1 binding sequence is GHE(X)2G(X)5G(X)2V located at amino acid residues 68-82, and Zn2 binding sequence GD(X)9,10C(X)2C(X)2(X)7C located at amino acid residues 88-114, structural zinc coordinated residue are Cys100, Cys103, Cys106, and Cys114
Zn2+
4 Zn2+ per homodimer, the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions
Zn2+
required; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling
Zn2+
-
restores activity after incubation in buffer containing a divalent-cation exchange resin
Zn2+
-
required, Zn1-binding motif [GHE(X)2G(X)5G(X)2 V] and Zn2-binding motif [GD(X)9,10C(X)2C(X)2C(X)7C] occur in most of the isozymes, overview
Zn2+
require, the TaCAD12 protein contains one alcohol dehydrogenase domain (42-157 aa) with two Zn binding sites (41-63 and 76-90 aa) and one Zn-binding dehydrogenase domain (199-323 aa)
additional information
slight activating effect by KCl at 100 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-monophosphate
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
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
coniferyl aldehyde
competitve, a stronger inhibitor than sinapyl aldehyde; competitve, a stronger inhibtior than sinapyl aldehyde; competitve, a stronger inhibtior than sinapyl aldehyde
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
-
sinapyl aldehyde
competitve, a weaker inhibitor than coniferyl aldehyde; competitve, a weaker inhibtior than coniferyl aldehyde; competitve, a weaker inhibtior than coniferyl aldehyde
Zn2+
-
inhibitory at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions, strong inhibition
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves results in reduced penetration resistance against Puccinia hordei infection
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves has no efffect in on resistance against Puccinia hordei infection
additional information
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
additional information
-
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
-
Cinnamyl alcohol dehydrogenase activity remains unaffected by both methyl jasmonate and salicylic acid. This indicates that methyl jasmonate and salicylic acid induce the accumulation of phenolic compounds in ginseng root by altering the phenolic synthesis enzymes
-
additional information
-
the enzyme is not nduced by stress, but is related to cell wall lignification
-
additional information
-
mechanical stress application induces a strong increase of CAD activity in rubbed internode with an approximately 2fold increase when compared to control tomato internodes. Increased activity of CAD is associated with a higher lignin content in the rubbed internode
-
additional information
-
CAD transcripts are accumulated in response to infection with Blumeria graminis f. sp. tritici. Accumulates at 6 hpi, followed by a slight decrease at 12 hpi and then a sharp increase at 24 hpi
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0244
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0891
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0042
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.013
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
0.036
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.114
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
0.117
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
0.0382
4-coumarylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
0.1122
4-coumarylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
0.09318
5-hydroxyconiferylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.152
5-hydroxyconiferylaldehyde
isoform CAD2, at pH 6.0 and 25°C
31
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
0.06592
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.09463
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.01425
cinnamaldehyde
pH 6.0, 30°C, recombinant enzyme
0.03115
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.08554
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.00098
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0075
coniferyl alcohol
; pH 8.8, temperature not specified in the publication
0.117
coniferyl alcohol
; pH 8.8, temperature not specified in the publication
0.0038
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0066
coniferyl aldehyde
-
wild-type Mt-CAD2, pH and temperature not specified in the publication
0.0068
coniferyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.0085
coniferyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0109
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.01996
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
0.02062
coniferyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme; pH 5.0, 30°C, recombinant His-tagged enzyme
0.0219
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.024
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0282
coniferyl aldehyde
pH 6.0, 30°C, recombinant enzyme
0.0289
coniferyl aldehyde
recombinant GST-tagged enzyme, pH and temperature not specified in the publication
0.032
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.146
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
0.008
p-coumaryl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0094
p-coumaryl aldehyde
-
wild-type Mt-CAD2, pH and temperature not specified in the publication
0.0272
p-coumaryl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.06095
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.09157
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.0156
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0043
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme; pH 5.0, 30°C, recombinant His-tagged enzyme
0.0058
sinapyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.0095
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.00985
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
0.0109
sinapyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0145
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.026
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0342
sinapyl aldehyde
recombinant GST-tagged enzyme, pH and temperature not specified in the publication
0.0406
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0471
sinapyl aldehyde
pH 6.0, 30°C, recombinant enzyme
0.055
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.235
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
0.279
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
0.283
sinapyl aldehyde
-
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
0.73
sinapyl aldehyde
-
wild-type Mt-CAD2, pH and temperature not specified in the publication
1.969
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
KJ159967
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
-
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
additional information
additional information
steady-state kinetics; steady-state kinetics; steady-state kinetics; steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.7
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.026
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
6.8
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
40.2
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
74.2
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.273
4-coumarylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
0.367
4-coumarylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
0.005
5-hydroxyconiferylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.007
5-hydroxyconiferylaldehyde
isoform CAD2, at pH 6.0 and 25°C
2.5
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
0.062
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.072
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.072
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.085
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
13.2
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.00098
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0121
coniferyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.032
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.1
coniferyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
7.78
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
8.68
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
9.1
coniferyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
45.42
coniferyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme; pH 5.0, 30°C, recombinant His-tagged enzyme
99.6
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
138
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
7564
coniferyl aldehyde
pH 6.0, 30°C, recombinant enzyme
0.46
p-coumaryl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
15.6
p-coumaryl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.005
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.006
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
46.4
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.00135
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0053
sinapyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.024
sinapyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
0.039
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
0.041
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.044
sinapyl aldehyde
-
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
0.083
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
3.63
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
10.09
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
10.2
sinapyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
16.59
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme; pH 5.0, 30°C, recombinant His-tagged enzyme
195
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
196
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.169
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.082
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
5880
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.23
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
345
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
523
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
2061
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
3.273
4-coumarylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
7.136
4-coumarylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
0.0448
5-hydroxyconiferylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.054
5-hydroxyconiferylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.766
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.935
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C