Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-dimethylcinnamyl alcohol + NADP+
2,4-dimethylcinnamaldehyde + NADPH
-
-
-
?
2-propanol + NADP+
? + NADPH + H+
-
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
3,4-methylenedioxycinnamyl alcohol + NADP+
3,4-methylenedioxycinnamaldehyde + NADPH
-
-
-
?
3-methoxybenzylalcohol + NADP+
3-methoxybenzaldehyde + NADPH
-
-
-
?
3-phenyl-1-propanol + NAD+
3-phenylpropanal + NADH + H+
-
-
-
-
r
4-bromocinnamyl alcohol + NADP+
4-bromocinnamaldehyde + NADPH
-
-
-
?
4-chlorocinnamyl alcohol + NADP+
4-chlorocinnamaldehyde + NADPH
-
-
-
?
4-coumaraldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
-
-
-
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
4-methoxybenzylalcohol + NADP+
4-methoxybenzaldehyde + NADPH
-
-
-
?
4-methoxycinnamyl alcohol + NADP+
4-methoxycinnamaldehyde + NADPH
-
-
-
?
4-methylcinnamyl alcohol + NADP+
4-methylcinnamaldehyde + NADPH
-
-
-
?
5-hydroxyconiferyl aldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
-
-
?
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
5-hydroxyconiferyl aldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
5-hydroxyconiferylaldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
-
-
?
5-hydroxyconiferylaldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
lowest catalytic efficiency
-
-
?
allyl alcohol + NAD+
prop-2-enal + NADH + H+
-
-
-
-
r
artemisinic aldehyde + NADPH + H+
artemisinic alcohol + NADP+
-
-
-
?
benzaldehyde + NADP+
benzoic acid + NADPH
-
the enzyme also shows dismutase activity
-
-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH
-
-
-
-
r
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
benzylaldehyde + NADPH + H+
slight activity
-
-
r
benzylalcohol + NADP+
benzaldehyde + NADPH
-
-
-
?
butanol + NADP+
butyraldehyde + NADPH
-
-
-
-
r
caffeoyl aldehyde + NADPH + H+
caffeoyl alcohol + NADP+
-
-
-
r
caffeyl aldehyde + NADPH
caffeyl alcohol + NADP+
-
-
-
r
caffeylaldehyde + NADP+
caffeyl alcohol + NADPH + H+
low activity
-
-
?
caffeylaldehyde + NADPH + H+
caffeyl alcohol + NADP+
-
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH + H+
-
-
-
?
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
coniferol + NADP+
coniferyl aldehyde + NADPH
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl aldehyde + NADPH
coniferol + NADP+
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
coumaryl alcohol + NADP+
coumaraldehyde + NADPH + H+
-
-
-
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
-
-
-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
-
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
p-coumarylaldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
?
propanol + NADP+
propionaldehyde + NADPH
-
-
-
-
r
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
sinapylaldehyde + NADPH + H+
sinapyl alcohol + NADP+
additional information
?
-
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
-
?
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
r
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
-
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
Erianthus sp. IK 76-81
-
-
-
-
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
-
-
-
-
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
-
-
-
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
-
-
-
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
-
-
-
?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
catalytic preference for 4-coumaraldehyde
-
-
?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
high catalytic efficiency
-
-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
-
-
-
-
r
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
CAD4 displays slight activity for benzoyl alcohol
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
-
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
-
-
-
r
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
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
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
-
-
-
r
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
key enzyme in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
involved in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
-
-
-
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
-
-
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
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
-
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
-
-
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Erianthus sp. IK 76-81
-
-
-
-
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
favourite substrate
-
-
?
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
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
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+
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Eucalyptus sp.
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
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 alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
?
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 alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
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 alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
?
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 alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
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
-
-
?
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
-
-
?
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
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH
coniferol + NADP+
-
-
-
-
?
coniferyl aldehyde + NADPH
coniferol + NADP+
-
-
-
?
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
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
coniferyl alcohol + NADP+
-
recombinant enzyme encoded by gene GH2
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Erianthus sp. IK 76-81
-
-
-
-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
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+
-
?
-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
?
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
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
?
-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
?
-
?
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-coumaraldehyde + NADPH
-
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
-
-
-
?
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 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+
-
-
-
?
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
r
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
-
?
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
?
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
?
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
-
-
-
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
only CAD-C isoform
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
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
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
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+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
preferred substrate
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
recombinant enzyme encoded by gene GH2
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
?
-
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
low activity
-
-
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
very low activity
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
-
?
sinapylaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
sinapylaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
?
additional information
?
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
substrate specificity of isozyme CAD5
-
-
?
additional information
?
-
substrate specificity of isozyme CAD5
-
-
?
additional information
?
-
-
substrate specificity of isozyme CAD5
-
-
?
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
?
-
-
substituted and unsubstituted benzaldehydes
-
-
?
additional information
?
-
-
enzyme involved in lignification in vascular plants
-
-
?
additional information
?
-
-
not: methanol, ethanol, n-propanol, n-butanol, isobutanol, geraniol, various aromatic alcohols (e.g. salicyl alcohol, vanillyl alcohol, piperonyl alcohol)
-
-
?
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
?
additional information
?
-
coniferylaldehyde and sinapylaldehyde are the preferred substrates
-
-
?
additional information
?
-
coniferylaldehyde and sinapylaldehyde are the preferred substrates
-
-
?
additional information
?
-
-
no activity with methanol and ethanol as alcoholic substrates
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
?
additional information
?
-
mo activity with sinapyl aldehyde
-
-
?
additional information
?
-
mo activity with sinapyl aldehyde
-
-
?
additional information
?
-
-
mo activity with sinapyl aldehyde
-
-
?
additional information
?
-
no activity with sinapaldehyde
-
-
?
additional information
?
-
no activity with sinapaldehyde
-
-
?
additional information
?
-
-
no activity with sinapaldehyde
-
-
?
additional information
?
-
-
gene GH2 encodes a multifunctional enzyme
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
not: sinapaldehyde, 4-hydroxybenzaldehyde, vanillin, 4-hydroxy-3,5-dimethoxybenzaldehyde, 3,4-dimethoxybenzaldehyde, salicylaldehyde, 2-methoxybenzaldehyde, mannose, acetaldehyde
-
-
?
additional information
?
-
-
final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
-
-
?
additional information
?
-
beta-glucuronidase expression driven by the CAD promoter is wound-inducible
-
-
?
additional information
?
-
-
beta-glucuronidase expression driven by the CAD promoter is wound-inducible
-
-
?
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
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
KJ159967
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
?
-
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
?
-
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
-
-
?
additional information
?
-
-
enzyme of lignification
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, 30°C
0.013 - 0.117
4-coumaraldehyde
0.00266 - 7.97
4-coumaryl aldehyde
0.0382 - 0.1122
4-coumarylaldehyde
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
0.09318 - 0.152
5-hydroxyconiferylaldehyde
0.04
acetaldehyde
-
pH 7.5, 37°C, recombinant enzyme
0.5
allyl alcohol
-
pH 8.0, 30°C
0.41 - 2.6
benzyl alcohol
9
butanol
-
pH 7.5, 37°C, recombinant enzyme
0.0891
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.06592 - 0.09463
caffeylaldehyde
0.0015 - 0.92
cinnamaldehyde
0.0038 - 0.27
cinnamyl alcohol
0.005 - 0.02825
cinnamyl aldehyde
0.00077 - 0.1136
coniferaldehyde
0.00098 - 0.677
coniferyl alcohol
0.0018 - 9.17
coniferyl aldehyde
0.0042
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
46
ethanol
-
pH 7.5, 37°C, recombinant enzyme
0.0012 - 0.03
p-coumaraldehyde
0.034 - 0.283
p-coumaryl alcohol
0.0035 - 0.0272
p-coumaryl aldehyde
13
Propanol
-
pH 7.5, 37°C, recombinant enzyme
0.0043 - 0.2082
sinapaldehyde
0.0062 - 0.56
sinapyl alcohol
0.00194 - 5.52
sinapyl aldehyde
additional information
additional information
-
0.0069
3,4-dimethoxycinnamaldehyde
-
-
0.043
3,4-dimethoxycinnamaldehyde
-
-
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
0.048
4-coumaraldehyde
-
-
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
0.00266
4-coumaryl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.00936
4-coumaryl aldehyde
isoform CAD2, at pH 6.3 and 30°C
0.01088
4-coumaryl aldehyde
isoform CAD6, at pH 6.3 and 30°C
0.01105
4-coumaryl aldehyde
at pH 7.5 and 30°C
0.06975
4-coumaryl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.0809
4-coumaryl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
0.268
4-coumaryl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
2.12
4-coumaryl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
4.18
4-coumaryl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
4.63
4-coumaryl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
6.88
4-coumaryl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
7.1
4-coumaryl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
7.97
4-coumaryl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
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
0.03
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme
31
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
0.41
benzyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
1
benzyl alcohol
-
CAD1 isoform
1
benzyl alcohol
-
isoform CAD1, pH and temperature not specified in the publication
2.6
benzyl alcohol
-
CAD2 isoform
2.6
benzyl alcohol
-
isoform CAD2, pH and temperature not specified in the publication
0.06592
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.09463
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.0015
cinnamaldehyde
-
pH 6.5, 40°C
0.0025
cinnamaldehyde
-
-
0.0053
cinnamaldehyde
-
-
0.0059
cinnamaldehyde
pH 6.5, 40°C
0.01425
cinnamaldehyde
pH 6.0, 30°C, recombinant enzyme
0.017
cinnamaldehyde
-
in 30 mM Tris-HCl (pH 8.0)
0.03
cinnamaldehyde
-
pH 7.5, 50°C
0.92
cinnamaldehyde
-
pH 8.0, 30°C
0.0038
cinnamyl alcohol
-
pH 8.8, 40°C
0.0113
cinnamyl alcohol
pH 8.8, 40°C
0.0122
cinnamyl alcohol
pH 8.8, 37°C
0.026
cinnamyl alcohol
-
-
0.1
cinnamyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
0.11
cinnamyl alcohol
-
pH 8.8, 50°C
0.156
cinnamyl alcohol
-
-
0.17
cinnamyl alcohol
-
pH 8.0, 30°C
0.27
cinnamyl alcohol
-
in 30 mM Tris-HCl (pH 8.0)
0.005
cinnamyl aldehyde
-
pH 7.5, 37°C, recombinant enzyme
0.0053
cinnamyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
0.01411
cinnamyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.02825
cinnamyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
0.00077
coniferaldehyde
-
-
0.0017
coniferaldehyde
-
-
0.0018
coniferaldehyde
-
-
0.0091
coniferaldehyde
-
-
0.012
coniferaldehyde
-
-
0.03115
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.0369
coniferaldehyde
-
isoform CAD1, at pH 7.5 and 30°C
0.0676
coniferaldehyde
-
isoform CAD3, at pH 7.5 and 30°C
0.0797
coniferaldehyde
-
isoform CAD4, at pH 7.5 and 30°C
0.08554
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.1136
coniferaldehyde
-
isoform CAD2, at pH 7.5 and 30°C
0.00098
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0014
coniferyl alcohol
-
with NADP+
0.005
coniferyl alcohol
-
pH 8.8, 40°C
0.0069
coniferyl alcohol
-
-
0.0075
coniferyl alcohol
-
0.0075
coniferyl alcohol
pH 8.8, temperature not specified in the publication
0.0096
coniferyl alcohol
pH 8.8, 40°C
0.011
coniferyl alcohol
-
-
0.0181
coniferyl alcohol
pH 8.8, 37°C
0.032
coniferyl alcohol
-
-
0.051
coniferyl alcohol
-
purified isoform CAD-C
0.11
coniferyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
0.117
coniferyl alcohol
-
0.117
coniferyl alcohol
pH 8.8, temperature not specified in the publication
0.14
coniferyl alcohol
-
CAD2 isoform
0.241
coniferyl alcohol
-
with NAD+
0.247
coniferyl alcohol
pH 6.25, 30°C, recombinant CAD1-1
0.325
coniferyl alcohol
pH 6.25, 30°C, recombinant CAD1-7
0.414
coniferyl alcohol
-
isoform CAD-B
0.52
coniferyl alcohol
-
CAD1 isoform
0.677
coniferyl alcohol
-
isoform CAD-A
0.0018
coniferyl aldehyde
-
-
0.0025
coniferyl aldehyde
-
CAD2 isoform
0.0037
coniferyl aldehyde
pH 6.5, 40°C
0.0038
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.00437
coniferyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
0.0044
coniferyl aldehyde
-
pH 8.8, 30°C, recombinant enzyme encoded by GH2
0.0045
coniferyl aldehyde
-
pH 6.5, 40°C
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
0.008
coniferyl aldehyde
-
pH 7.5, 37°C, recombinant enzyme
0.0085
coniferyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0104
coniferyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
0.01076
coniferyl aldehyde
at pH 7.5 and 30°C
0.0109
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.01144
coniferyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.01618
coniferyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
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
0.0214
coniferyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
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
0.027
coniferyl aldehyde
-
CAD1 isoform
0.028
coniferyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
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
0.031
coniferyl aldehyde
pH 8.8, 30°C, recombinant CAD1-7
0.032
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.053
coniferyl aldehyde
pH 10.5, 30°C, recombinant CAD1-1
0.068
coniferyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
0.09518
coniferyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.146
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
0.233
coniferyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
0.387
coniferyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
5.68
coniferyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
9.17
coniferyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
0.052
NAD+
-
pH 8.0, 30°C
0.016
NADH
-
pH 7.5, 50°C
0.0038
NADP+
-
-
0.0057
NADP+
pH 8.8, 40°C
0.0085
NADP+
-
pH 8.8, 40°C
0.06
NADP+
-
pH 7.5, 37°C, recombinant enzyme, with benzyla alcohol
0.0015
NADPH
-
pH 6.5, 40°C
0.0025
NADPH
pH 6.5, 40°C
0.0046
NADPH
-
with coniferaldehyde
0.0067
NADPH
-
with cinnamaldehyde
0.15
NADPH
-
pH 7.5, 37°C, recombinant enzyme, with acetaldehyde
0.0012
p-coumaraldehyde
-
-
0.0091
p-coumaraldehyde
-
-
0.03
p-coumaraldehyde
-
-
0.034
p-coumaryl alcohol
-
isoform CAD-C
0.046
p-coumaryl alcohol
-
purified isoform CAD-C
0.057
p-coumaryl alcohol
-
-
0.132
p-coumaryl alcohol
-
-
0.15
p-coumaryl alcohol
-
isoform CAD-B
0.27
p-coumaryl alcohol
-
CAD1 isoform
0.283
p-coumaryl alcohol
-
isoform CAD-A
0.0035
p-coumaryl aldehyde
pH 6.5, 40°C
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
0.0043
sinapaldehyde
-
-
0.04792
sinapaldehyde
-
isoform CAD1, at pH 7.5 and 30°C
0.06095
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.09157
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.1378
sinapaldehyde
-
isoform CAD2, at pH 7.5 and 30°C
0.1699
sinapaldehyde
-
isoform CAD4, at pH 7.5 and 30°C
0.2082
sinapaldehyde
-
isoform CAD3, at pH 7.5 and 30°C
0.0062
sinapyl alcohol
-
pH 8.8, 40°C
0.0086
sinapyl alcohol
pH 8.8, 40°C
0.0156
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0166
sinapyl alcohol
-
-
0.0238
sinapyl alcohol
pH 8.8, 37°C
0.054
sinapyl alcohol
-
purified isoform CAD-C
0.062
sinapyl alcohol
-
isoform CAD-C
0.067
sinapyl alcohol
-
isoform CAD-B
0.24
sinapyl alcohol
-
CAD2 isoform
0.56
sinapyl alcohol
-
CAD1 isoform
0.00194
sinapyl aldehyde
at pH 7.5 and 30°C
0.0028
sinapyl aldehyde
pH 6.5, 40°C
0.0043
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
0.005
sinapyl aldehyde
-
CAD2 isoform
0.0058
sinapyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.00642
sinapyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.0072
sinapyl aldehyde
-
-
0.0078
sinapyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
0.00819
sinapyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
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
0.01072
sinapyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
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
0.0168
sinapyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
0.0208
sinapyl aldehyde
-
pH 8.8, 30°C, recombinant enzyme encoded by GH2
0.026
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.033
sinapyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
0.0342
sinapyl aldehyde
recombinant GST-tagged enzyme, pH and temperature not specified in the publication
0.035
sinapyl aldehyde
-
CAD1 isoform
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
0.05976
sinapyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.0783
sinapyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
0.0793
sinapyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
0.105
sinapyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
0.112
sinapyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
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
5.52
sinapyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
KJ159967
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11.2
3-Phenyl-1-propanol
-
pH 8.0, 30°C
0.026 - 74.2
4-coumaraldehyde
0.069 - 30.16
4-coumaryl aldehyde
0.273 - 0.367
4-coumarylaldehyde
0.005 - 0.007
5-hydroxyconiferylaldehyde
16.7
acetaldehyde
-
pH 7.5, 37°C, recombinant enzyme
32.9
allyl alcohol
-
pH 8.0, 30°C
8.4
benzyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
5.7
butanol
-
pH 7.5, 37°C, recombinant enzyme
0.062 - 0.072
caffeylaldehyde
5.63 - 1437
cinnamaldehyde
6.41 - 60.78
cinnamyl alcohol
0.188 - 9.05
cinnamyl aldehyde
0.072 - 12
coniferaldehyde
0.43 - 16.3
coniferyl alcohol
0.00098 - 7564
coniferyl aldehyde
24.7
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
7.1
ethanol
-
pH 7.5, 37°C, recombinant enzyme
0.46 - 22.5
p-coumaryl aldehyde
12.8
Propanol
-
pH 7.5, 37°C, recombinant enzyme
0.005 - 8.3
sinapaldehyde
14.38 - 46.4
sinapyl alcohol
0.00135 - 9368
sinapyl aldehyde
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
0.069
4-coumaryl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.076
4-coumaryl aldehyde
isoform CAD6, at pH 6.3 and 30°C
1.08
4-coumaryl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
1.19
4-coumaryl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
2.17
4-coumaryl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
3.03
4-coumaryl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
3.27
4-coumaryl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
3.59
4-coumaryl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
9.5
4-coumaryl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
11.93
4-coumaryl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
12.36
4-coumaryl aldehyde
at pH 7.5 and 30°C
13.86
4-coumaryl aldehyde
isoform CAD2, at pH 6.3 and 30°C
30.16
4-coumaryl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
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
2.3
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme
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
5.63
cinnamaldehyde
-
pH 6.5, 40°C
14.4
cinnamaldehyde
-
pH 8.0, 30°C
18
cinnamaldehyde
pH 6.5, 40°C
55
cinnamaldehyde
-
pH 7.5, 50°C
107.9
cinnamaldehyde
-
in 30 mM Tris-HCl (pH 8.0)
1437
cinnamaldehyde
pH 6.0, 30°C, recombinant enzyme
6.41
cinnamyl alcohol
-
pH 8.8, 40°C
13.3
cinnamyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
16.2
cinnamyl alcohol
pH 8.8, 40°C
18.1
cinnamyl alcohol
-
pH 8.0, 30°C
43
cinnamyl alcohol
-
pH 8.8, 50°C
60.78
cinnamyl alcohol
-
in 30 mM Tris-HCl (pH 8.0)
0.188
cinnamyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.311
cinnamyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
7.7
cinnamyl aldehyde
-
pH 7.5, 37°C, recombinant enzyme
9.05
cinnamyl aldehyde
isoform CAD2, at pH 6.3 and 30°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
7.9
coniferaldehyde
-
isoform CAD1, at pH 7.5 and 30°C
9
coniferaldehyde
-
isoform CAD2, at pH 7.5 and 30°C
10.8
coniferaldehyde
-
isoform CAD4, at pH 7.5 and 30°C
12
coniferaldehyde
-
isoform CAD3, at pH 7.5 and 30°C
0.43
coniferyl alcohol
pH 6.25, 30°C, recombinant CAD1-1
0.99
coniferyl alcohol
pH 6.25, 30°C, recombinant CAD1-7
3.5
coniferyl alcohol
-
pH 7.5, 37°C, recombinant enzyme
8.75
coniferyl alcohol
-
pH 8.8, 40°C
13.2
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
16.3
coniferyl alcohol
pH 8.8, 40°C
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
0.154
coniferyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
0.17
coniferyl aldehyde
pH 10.5, 30°C, recombinant CAD1-1
0.24
coniferyl aldehyde
pH 8.8, 30°C, recombinant CAD1-7
0.284
coniferyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.76
coniferyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
1.3
coniferyl aldehyde
-
pH 8.8, 30°C, recombinant enzyme encoded by GH2
2 - 3.7
coniferyl aldehyde
pH 6.5, 40°C
2.33
coniferyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
3.68
coniferyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
3.76
coniferyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
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
9.26
coniferyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
12.77
coniferyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
13.82
coniferyl aldehyde
at pH 7.5 and 30°C
16.56
coniferyl aldehyde
-
pH 6.5, 40°C
20.28
coniferyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
25.83
coniferyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
27.4
coniferyl aldehyde
-
pH 7.5, 37°C, recombinant enzyme
30.13
coniferyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
45.42
coniferyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
71.57
coniferyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
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
0.0242
NAD+
-
-
0.0555
NADP+
-
-
9.22
NADP+
-
pH 8.8, 40°C
15.5
NADP+
-
pH 7.5, 37°C, recombinant enzyme, with benzyla alcohol
0.49
NADPH
-
-
15.31
NADPH
-
pH 6.5, 40°C
25.2
NADPH
-
pH 7.5, 37°C, recombinant enzyme, with acetaldehyde
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
22.5
p-coumaryl aldehyde
pH 6.5, 40°C
0.005
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.006
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
2.4
sinapaldehyde
-
isoform CAD3, at pH 7.5 and 30°C
2.76
sinapaldehyde
-
isoform CAD4, at pH 7.5 and 30°C
3.4
sinapaldehyde
-
isoform CAD2, at pH 7.5 and 30°C
8.3
sinapaldehyde
-
isoform CAD1, at pH 7.5 and 30°C
14.38
sinapyl alcohol
-
pH 8.8, 40°C
16
sinapyl alcohol
pH 8.8, 40°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
0.073
sinapyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
0.083
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
0.128
sinapyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
1.05
sinapyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
1.59
sinapyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
2.5
sinapyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
3.32
sinapyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
3.4
sinapyl aldehyde
-
pH 8.8, 30°C, recombinant enzyme encoded by GH2
3.63
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
5.29
sinapyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
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
12.54
sinapyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
14.03
sinapyl aldehyde
at pH 7.5 and 30°C
16.59
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
18.98
sinapyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
31.75
sinapyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
32.2
sinapyl aldehyde
pH 6.5, 40°C
39.97
sinapyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
41.19
sinapyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
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
9368
sinapyl aldehyde
pH 6.0, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
shell zone, immunogold-electron microscopy of shoot apex
brenda
-
from leaves
brenda
-
-
brenda
-
CAD is accumulated in the epidermis, CAD gene expression after pathogen attack is predominantly in the epidermis
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
expression of isoforms Cad-2, Cad-3
brenda
-
-
brenda
-
-
brenda
-
young
brenda
-
brenda
-
-
brenda
-
immunogold-electron microscopy of shoot apex
brenda
-
developing, immunogold-electron microscopy of shoot apex
brenda
-
immunogold-electron microscopy of mature stems
brenda
-
brenda
-
brenda
-
immunogold-electron microscopy of shoot apex
brenda
-
brenda
-
young
brenda
-
brenda
-
brenda
-
differentiating element
brenda
-
predominant expression of isoforms Cad-1, Cad-9
brenda
-
of 32 single nucleotide polymorphisms in the coding region of CAD, 28 single nucleotide polymorphisms are detected in Acacia auriculiformis A3 x Acacia mangium M22 parental combination and 22 single nucleotide polymorphisms are detected in Acacia auriculiformis A6 x Acacia mangium M20 parental combination
brenda
-
of 32 single nucleotide polymorphisms in the coding region of CAD, 28 single nucleotide polymorphisms are detected in Acacia auriculiformis A3 x Acacia mangium M22 parental combination and 22 single nucleotide polymorphisms are detected in Acacia auriculiformis A6 x Acacia mangium M20 parental combination
brenda
-
all CAD genes expressed, but at different levels. Very low expression of CAD7
brenda
-
brenda
-
brenda
highest expression level in buds
brenda
very high expression level in buds
brenda
-
-
brenda
-
from xylem strings of shoots of a three-year-old tree
brenda
-
sap
brenda
-
immunogold-electron microscopy of mature stems
brenda
-
-
brenda
-
xylem-derived
brenda
-
-
brenda
-
brenda
-
-
brenda
-
from roots
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
brenda
highest CAD1 expression level in mature flowers
brenda
-
-
brenda
expression in all fruit ripening stages
brenda
-
high levels of CAD activity/expression in Sanguinella, a blood flesh cultivar, phenolics and lignin contents and CAD activities, overview
brenda
-
-
brenda
-
-
brenda
Bmr6 expression in young internodes is significantly higher than CAD4 for all genotypes
brenda
Bmr6 expression in young internodes is significantly higher than CAD4 for all genotypes, but only 4fold to 5fold higher in bmr6 and bmr6 bmr12 internodes. Bmr6 expression is significantly decreased in bmr6 and bmr6 bmr12 compared to the wild-type and bmr12, 20fold and 15fold, respectively
brenda
-
brenda
-
brenda
low enzyme level
brenda
-
sheaths and leaf blades
brenda
-
brenda
-
low activity
brenda
-
brenda
highest expression of isoforms CAD3, CAD5, CAD6 and CAD8
brenda
young and old, veins
brenda
-
brenda
FC1 is expressed slightly more at the seedling stage than at the heading stage
brenda
-
all CAD genes expressed, but at different levels. CAD13, CAD7,CAD12 are most highly expressed in leaves. CAD9 is preferentially expressed in leaves and xylem
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
low expression
brenda
-
-
brenda
-
brenda
-
brenda
young
brenda
-
all CAD genes expressed, but at different levels
brenda
-
brenda
-
brenda
-
brenda
-
isoforms Cad-4, Cad-5, expression in root caps. Isoforms Cad-2, Cad-3, expression in non-lignifying root tips
brenda
-
brenda
constitutively expressed
brenda
-
brenda
-
promoter expression is strong in the roots. Promoter activity increases with increasing root age, and strong promoter expression is observed in the lateral root emergence sites and in root tips
brenda
-
promoter expression is strong in the roots. Promoter activity increases with increasing root age, and strong promoter expression is observed in the lateral root emergence sites and in root tips
-
brenda
mature
brenda
-
-
brenda
-
brenda
FC1 is expressed slightly more at the seedling stage than at the heading stage
brenda
-
-
brenda
-
root suspension culture, 40 day-old adventitious root
brenda
-
brenda
-
brenda
greatest expression in the root
brenda
-
-
brenda
-
-
brenda
quantitative realtime PCR enzyme expression analysis during seed development, overview. CAD2 shows the highest expression level of all three CAD isozymes in Carthamus tinctorius
brenda
-
developing
brenda
-
brenda
-
brenda
highest expression of isoforms CAD2 and CAD6
brenda
-
etiolated young shoot
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
elongating
brenda
-
isoforms Cad-4, Cad-5, Cad-7, Cad-8, expression in lignifying stem tissue. No expression of isoforms Cad-2, Cad-3 in lignifying tissue
brenda
highly expressed in developing stem. Of the seven CAD genes identified in Brachypodium distachyon, BdCAD1 expression is greatest in stem tissue, exhibiting 10fold higher transcript level than any of the other seven BdCAD genes
brenda
-
brenda
low expression of CAD3 in stem
brenda
Erianthus sp. IK 76-81
-
-
brenda
-
young section
brenda
constitutively expressed
brenda
-
brenda
highest CAD2 expression level in stems
brenda
-
-
brenda
-
brenda
-
brenda
highest expression of isoform CAD4
brenda
-
-
-
brenda
-
brenda
-
brenda
FC1 is expressed slightly more at the seedling stage than at the heading stage. At the heading stage, a strong FC1 expression level in the first internode
brenda
-
brenda
-
mature stem
brenda
-
-
brenda
-
-
brenda
-
internode
brenda
mRNA is more abundant in the lower stem than in the upper stem
brenda
high expression
brenda
transcriptional patterns of TaCAD12 in wheat stems after Rhizoctonia cerealis inoculation analyzed by quantitative RT-PCR, overview
brenda
-
brenda
-
secondary
brenda
LtuCAD1 has the highest expression level in xylem
brenda
-
-
brenda
the native CAD gene is preferentially expressed in differentiating xylem both in stems and roots
brenda
-
-
brenda
-
differentiating tissue
brenda
-
-
brenda
-
brenda
-
young, immunogold-electron microscopy of mature stems
brenda
-
all CAD genes expressed, but at different levels. CAD4 and CAD10 are strongly expressed in xylem, with CAD10 more expressed. CAD4 and CAD10 are 100 times more highly expressed than the other CAD genes. Very low expression of CAD7. CAD9 is preferentially expressed in leaves and xylem
brenda
-
-
brenda
-
-
brenda
additional information
enzyme expression pattern of AtCAD-C and AtCAD-D, no expression in silique
brenda
additional information
-
quantitative RT-PCR expression analysis, in the Bd4179 mutant, only internodes and peduncles show detectable activity
brenda
additional information
-
differential expression of CmCADs
brenda
additional information
-
differential expression of CmCADs, and CmCAD5 is expressed in different vegetative tissues except mature leaves, with the highest expression in flower, and CmCAD5 is strongly expressed in flesh during development
brenda
additional information
-
differential expression of CmCADs, CmCAD2 is strongly expressed in flesh during development
brenda
additional information
tissue expression study, no enzyme expression in root
brenda
additional information
-
tissue expression study, no enzyme expression in root
brenda
additional information
CAD expression pattern during different developmental stages, overview. HcCAD2 expression level is always higher than the expression level of HcCAD1. High expression levels in early stages of stem development and in mature stage of flowers development
brenda
additional information
CAD expression pattern during different developmental stages, overview. HcCAD2 expression level is always higher than the expression level of HcCAD1. High expression levels in early stages of stem development and in mature stage of flowers development
brenda
additional information
-
promoter expression is barely detecable in cotyledons. Weak expression is observed in lignified tissues of vascular system of mature leaves and stems
brenda
additional information
-
promoter expression is barely detecable in cotyledons. Weak expression is observed in lignified tissues of vascular system of mature leaves and stems
-
brenda
additional information
quantitative RT-PCR enzyme expression analysis. LtuCAD1 is differentially expressed in vascular tissues
brenda
additional information
main expression in sclerenchyma cell of secondary cell wall and vascular bundle region. Panicle, at the heading stage, show strong FC1 expression level
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. No obvious expression variation in the expression of PtoCAD8, PtoCAD8 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
-
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
KJ159967
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
-
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
-
CAD2, CAD3, CAD5, CAD6, CAD11, CAD14, CAD15 show no significant expression differences between tissues
brenda
additional information
-
in silico analysis of CAD genes
brenda
additional information
-
polymorphic restriction site is present in the near-isogenic lines Atlas bmr6, RTx430 bmr6, and Wheatland bmr6 and is absent from wild-type Atlas, RTx430, and Wheatland
brenda
additional information
polymorphic restriction site is present in the near-isogenic lines Atlas bmr6, RTx430 bmr6, and Wheatland bmr6 and is absent from wild-type Atlas, RTx430, and Wheatland
brenda
additional information
polymorphic restriction site is present in the near-isogenic lines Atlas bmr6, RTx430 bmr6, and Wheatland bmr6 and is absent from wild-type Atlas, RTx430, and Wheatland
brenda
additional information
no expression in root detectable
brenda
additional information
-
no expression in root detectable
brenda
additional information
-
transcriptional levels of TaCAD12 in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
brenda
additional information
transcriptional levels of TaCAD12 in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
brenda
additional information
-
neoformed calli induced by Agrobacterium rhizogenes on Phaseolus hypocotyl
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
a total of 24 putative full-length PRUPE_CAD genes are identified (in silico analysis) in the peach genome, overview
evolution
CAD tends to exist in multi-gene families with one gene being primarily responsible for lignin biosynthesis. The BdCAD family consists of Bradi3g06480 (BdCAD1), Bradi3g17920 (BdCAD2), Bradi3g22980 (BdCAD3), Bradi4g29770 (BdCAD4), Bradi4g29780 (BdCAD5), Bradi5g04130 (BdCAD6), and Bradi5g21550 (BdCAD7)
evolution
-
enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily, the SDR108E family together with a SDR115E daughter branch. Mt-CAD2 resides in the flowering plant phenylacetaldehyde-reductase subgroup. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1
evolution
-
enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1
evolution
flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
evolution
LtuCAD is a member of a multigene family that belongs to the medium-chain dehydrogenase/reductase superfamily. Sequence identity and similarity among Arabidopsis thaliana and Liriodendron tulipifera CAD protein homologues, overview
evolution
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties
evolution
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties. Isozyme PtoCAD12 is the only protein in the group III, as it is distinct from other PtoCADs and closely related to PoptrCAD12, AtCAD1 and OsCAD1
evolution
-
purified CAD by MALDI-TOF shows a significant homology to alcohol dehydrogenases of MDR superfamily
evolution
TaCAD12 belongs to IV group in CAD family, phylogenetic analysis
evolution
-
the phylogenetic tree reveals seven groups of CAD and melon CAD genes fall into four main groups. CmCAD1 and CmCAD2 belong to the bona fide CAD group, in which these CAD genes, as representative from angiosperms, are involved in lignin synthesis. Other CmCADs are distributed in group II, V and VII, respectively
evolution
-
flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
-
malfunction
CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting
malfunction
disruption of the genes encoding both cinnamyl alcohol dehydrogenases (CADs), including CADC and CADD, in Arabidopsis thaliana results in the atypical incorporation of hydroxycinnamaldehydes into lignin. The cadc/cadd-deficient and ferulic acid hydroxylase1 (fah1) cadc/cadd-deficient plants are similar in growth to wild-type plants even though their lignin compositions are drastically altered. In contrast, disruption of CAD in the F5H-overexpressing background results in dwarfism. The dwarfed phenotype observed in these plants does not appear to be related to collapsed xylem, a hallmark of many other lignin-deficient dwarf mutants. Mutant cadc/cadd-deficient and fah1 cadc/cadd-deficient, and cadd-deficient-F5H-overexpressing plants have increased enzyme-catalyzed cell wall digestibility
malfunction
-
in CAD1 mutants Bd4179 and Bd7591, the mature stems displaye reduced CAD activity and lower lignin content. Their lignins are enriched in 8-O-4- and 4-O-5-coupled sinapaldehyde units, as well as resistant inter-unit bonds and free phenolic groups. By contrast, there is no increase in coniferaldehyde end groups. Saccharification assays reveal that Bd4179 and Bd7591 lines are more susceptible to enzymatic hydrolysis than wild-type plants. The Bdcad1 alleles are responsible for the reddish-brown phenotype, overview. Wild-type BdCAD1 rescues the altered lignin profile of Arabidopsis and Brachypodium CAD mutants. Saccharification yields are improved in Bdcad1 mutant lines but biomass yield is not compromised
malfunction
knock-down of TaCAD12 transcript significantly represses resistance of the gene-silenced wheat plants to sharp eyespot caused by Rhizoctonia cerealis, whereas TaCAD12 overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot. Certain defense genes (Defensin, PR10, PR17c, and Chitinase1) and monolignol biosynthesis-related genes (TaCAD1, TaCCR, and TaCOMT1) are upregulated in the TaCAD12-overexpressing wheat plants but downregulated in TaCAD12-silencing plants
malfunction
loss of function of cinnamyl alcohol dehydrogenase 1 leads to unconventional lignin and a temperature-sensitive growth defect in Medicago truncatula. Insertion mutants Medicago truncatula show reduced lignin autofluorescence under UV microscopy and red coloration in interfascicular fibers. The phenotype is caused by insertion of retrotransposons into a gene annotated as encoding cinnamyl alcohol dehydrogenase, CAD1. NMR analysis indicates that the lignin is derived almost exclusively from coniferaldehyde and sinapaldehyde and is therefore strikingly different from classical lignins, which are derived mainly from coniferyl and sinapyl alcohols. Despite such a major alteration in lignin structure, the plants appear normal under standard conditions in the greenhouse or growth chamber.The plants are dwarfed when grown at 30°C. Glycome profiling reveals an increased extractability of some xylan and pectin epitopes from the cell walls of the cad1-1 mutant but decreased extractability of others, suggesting that aldehyde-dominant lignin significantly alters cell wall structure
malfunction
transgenic silencing of BdCAD1 causes altered flowering time and increases stem count and weight. Downregulation of BdCAD1 causes a leaf brown midrib phenotype. While acetyl bromide soluble lignin measurements are equivalent in BdCAD1 downregulated and control plants, histochemical staining and thioacidolysis indicate a decrease in lignin syringyl units and reduced syringyl/guaiacyl ratio in the transgenic plants. The perturbed enzyme results in greater stem biomass yield and bioconversion efficiency
malfunction
enzyme downregulation or knockout causes a reduction of lignin, which leads to severe plant dwarfism and a decreased biomass as well as decreased plant resistance to pathogens
malfunction
-
enzyme downregulation results in a significant decrease in both elastic modulus and yield stress while wood density and cellulose microfibril angle are not affected. Enzyme-downregulated poplars show increased incorporation of hydroxycinnamaldehydes. Enzyme downregulation results in red xylem tissue
malfunction
-
isoform CAD2 downregulation improves saccharification efficiency. CAD2 enzyme-deficient mutants accumulate feruloyl and sinapoyl hexose conjugates. The total amount of lignin is reduced in the mutants, and only minor amounts of hydroxycinnamaldehydes are incorporated. Oligolignols composed of coniferyl and sinapyl alcohols are reduced, whereas those with one sinapaldehyde unit are increased in abundance in cad2 mutants
malfunction
-
CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting
-
metabolism
-
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
-
cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis
metabolism
cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis and catalyzes the final step in the synthesis of monolignols
metabolism
cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase catalyze key steps in the pathway of lignin monomer biosynthesis
metabolism
cinnamyl alcohol dehydrogenase is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
metabolism
enzyme CAD catalyzes the final step in monolignol biosynthesis, leading to lignin formation in plants
metabolism
enzyme CAD is involved in the lignin biosynthesis. CAD converts cinnamylaldehyde to cinnamyl alcohol in the final step of the monolignol biosynthesis pathway and is a key enzyme in the pathway. The monolignol biosynthesis is the first major step in lignin biosynthesis, and crosslinkage of monolignols by perocidases and laccases is the second major step
metabolism
key enzyme in the biosynthesis of lignin. Artemisinin, arteannuin B, and other sesquiterpenes are profiled in the leaves of enzyme-overexpressing vs. wild-type plants
metabolism
the enzyme is responsible for lignin biosynthesis
metabolism
-
cinnamyl alcohol dehydrogenase is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
-
physiological function
CAD1 is the predominant CAD in wheat stem for lignin biosynthesis and is critical for lodging resistance
physiological function
-
after repression of cinnamyl alcohol dehydrogenase by RNAi, cell walls of plant stems contain a lignin polymer with a slight reduction in the S-to-G ratio without affecting the total lignin content. These cell walls accumulate higher levels of cellulose and arabinoxylans. In contrast, cell walls of midribs present a reduction in the total lignin content and of cell wall polysaccharides in RNAi-treated plants. Although to a different extent, the changes induced by the repression of CAD activity produce midribs and stems more degradable than wild-type plants. Cinnamyl alcohol dehydrogenase-RNAi-treated plants grown in the field present a wild-type phenotype and produce higher amounts of dry biomass and higher levels of ethanol compared to wild-type
physiological function
the change in lignin content has some linear correlation with the expression level of isoform CAD1 mRNA in different tissues
physiological function
enzyme overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot caused by the necrotrophic fungus Rhizoctonia cerealis
physiological function
the enzyme plays a role in lignin biosynthesis and the defencedefence of abiotic stresses
physiological function
-
CAD catalyzes the synthesis of coniferyl alcohol and sinapyl alcohol from coniferaldehyde (CAld) and sinapaldehyde respectively. Coniferyl alcohol can produce both lignin and lignan while sinapyl alcohol produces only lignin. Accumulation of ptox and lignin in PhCAD1-4 isoforms overexpressing transgenic lines, overview. Podophyllotoxin (ptox) is a therapeutically important lignan with economic importance derived from Podophyllum hexandrum and is used as a precursor for the synthesis of anticancer drugs etoposide, teniposide and etopophose
physiological function
-
cinnamyl alcohol dehydrogenase (CAD) catalyses the final step of the lignin biosynthesis, the conversion of cinnamyl aldehydes to alcohols, using NADPH as a cofactor. CAD2 may be involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network, and CmCAD2 is the main CAD enzymes for lignification of melon flesh
physiological function
-
cinnamyl alcohol dehydrogenase (CAD) catalyses the final step of the lignin biosynthesis, the conversion of cinnamyl aldehydes to alcohols, using NADPH as a cofactor. CAD3 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network
physiological function
-
cinnamyl alcohol dehydrogenase (CAD) catalyses the final step of the lignin biosynthesis, the conversion of cinnamyl aldehydes to alcohols, using NADPH as a cofactor. CmCAD1 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network
physiological function
-
cinnamyl alcohol dehydrogenase (CAD) catalyses the final step of the lignin biosynthesis, the conversion of cinnamyl aldehydes to alcohols, using NADPH as a cofactor. CmCAD5 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network, CmCAD5 may also function in flower development
physiological function
-
cinnamyl alcohol dehydrogenase catalyzes the reversible conversion of hydroxycinnamyl aldehydes to their corresponding alcohols, before their oxidative polymerization to lignin, a major constituent of the plant cell wall
physiological function
cinnamyl-alcohol dehydrogenase functions in one of the final steps of monolignol biosynthesis that catalyzes the reduction of cinnamyl aldehyde to cinnamyl alcohol prior to polymerization into the lignin polymer. It appears that BdCAD1 (Bradi3g06480) contains the conserved functional and structural features of a medium chain dehydrogenase/reductase specific to enzymes involved in lignin biosynthesis in secondary cell walls
physiological function
-
CmCAD4 may be a pseudogene
physiological function
enzyme CAD plays a role in defense responses to necrotrophic or soil-borne pathogens in wheat
physiological function
hydroxycinnamaldehyde content is a more important determinant of digestibility than lignin content
physiological function
-
involvement of BdCAD1 in lignification. Wild-type BdCAD1 rescues the altered lignin profile of Arabidopsis and Brachypodium CAD mutants
physiological function
isozymes PtoCAD1, -2, and -8 function differently depending on the cellular environment
physiological function
PtoCAD9 expression is very high in the bud, suggesting that it might be related to bud development
physiological function
-
the enzyme CAD activity is related to neither lignification nor differences in flesh firmness in the cultivars non-melting flesh Oro A/melting flesh Springcrest and Sanguinella, and color, blood-flesh Sanguinella, but might play a role in fruit ripening
physiological function
the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defence of abiotic stress in Plagiochasma appendiculatum
physiological function
the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defencedefence of abiotic stress in Plagiochasma appendiculatum
physiological function
When expressed in the Arabidopsis cad4 cad5 double mutant, LtuCAD1 is able to restore the total lignin content and decrease the S/G lignin ratio
physiological function
isoform CAD6 is involved in developmental lignification in rice and also plays a role in the defense response against rice pathogens
physiological function
isoforms CAD1 and 2 take part in the lignification of maturing stem and in the response to cold and drought stress
physiological function
isoforms CAD2 is involved in developmental lignification in rice and also plays a role in the defense response against rice pathogens
physiological function
-
the enzyme is involved in lignification
physiological function
-
the enzyme performs cadmium absorption and fixation to lignified cell wall during stress conditions. Enzyme-overexpressing plants exhibit higher cadmium tolerance compared to the wild type with higher chlorophyll and proline contents and antioxidant enzyme activity, as well as a lower methane dicarboxylic aldehyde content, electric conductivity and reactive oxygen species when exposed to cadmium stress due to a lower amount of Cd distributed in the cytoplasm
additional information
-
enzyme molecular docking analysis with substrates, active site structure, structure comparisons between isozymes, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
KJ159967
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
-
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
KJ159967
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
-
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
lignin and sugar content and composition during stem development, overview
additional information
lignin and sugar content and composition during stem development, overview
additional information
only BdCAD1 contains both active substrate binding residues, W119 and F298, which determine specificity for aromatic alcohols, and the conserved S212 residue that determines NADP(H) binding at that position
additional information
-
only BdCAD1 contains both active substrate binding residues, W119 and F298, which determine specificity for aromatic alcohols, and the conserved S212 residue that determines NADP(H) binding at that position
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
KJ159967
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
-
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
-
the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Mmolecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, structural modeling of Mt-CAD1, overview
additional information
-
the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Molecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, binding pockets for NADP(H) co-substrate and phenolic-aldehyde substrate in Mt-CAD2, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D57A
about 4fold increase in catalytic efficiency
H52A
about 40% decrease in catalytic efficiency
T49A
less than 0.5% of wild-type activity. Thermodynamic data indicate a negative enthalpic change, as well as a significant decrease in binding affinity with NADPH. Residue Thr49 is essential for overall catalytic conversion
G575A/G192D
-
the nucleotide substitution G575A occurs in BdCAD1 of the Bd4179 line, and consequently induces the G192D change in the highly conserved glycine-rich NADPH binding site GLGGVG
S212D
-
site-directed mutagenesis and overexpression in Escherichia coli
F226A
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 4fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
K169A
-
site-directed mutagenesis, inactive mutant
S130A
-
site-directed mutagenesis, inactive mutant
Y136F
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Y136F/F226A
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Y165A
-
site-directed mutagenesis, inactive mutant
Y165F
-
site-directed mutagenesis, inactive mutant
A278V
the isoform CAD4 mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme
G301F
the isoform CAD4 mutant enzyme displays slightly elevated Km values for 4-coumaryl aldehyde but decreased Km for coniferyl aldehyde compared with those values of wild type. The mutant becomes more dedicated toward sinapyl aldehyde, with substantially decreased efficiency for coniferyl aldehyde compared to the wild type enzyme
L119W
the isoform CAD4 mutant displays a slightly reduced Km value for both 4-coumaryl aldehyde and coniferyl aldehyde compared to the wild type enzyme. The mutant becomes more efficient toward coniferaldehyde due to the very small Km value, with substantially decreased efficiency for both sinapyl aldehyde and 4-coumaryl aldehyde
L119W/G301F
the isoform CAD4 double mutant displays its substrate preference in the order coniferyl aldehyde over 4-coumaryl aldehyde over sinapyl aldehyde, with higher catalytic efficiency than that of wild type enzyme. The mutant displays 10 and 800fold increases in its catalytic efficiency for coniferyl aldehyde and 4-coumaryl aldehyde, respectively, and a 50% decrease in catalytic efficiency for sinapyl aldehyde as compared to the wild type enzyme
Q132Stop
mutation responsible for the bmr6 phenotype. Mutation leads to significant reduction in all three main lignin subunits, H-, G-, and S-lignin of 4.8-, 7.3-, and 17.7fold, respectively, relative to the wild type. Lignin subunits S-indene and G-indene are elevated 9.5- and 8.3fold, respectively, in bmr6 relative to the wild type
W58L
the isoform CAD4 mutant enzyme displays slightly elevated Km values for 4-coumaryl aldehyde but decreased Km for coniferyl aldehyde compared with those values of wild type
Y288P
the isoform CAD4 mutant becomes more dedicated toward sinapyl aldehyde, with substantially decreased efficiency for coniferyl aldehyde compared to the wild type enzyme
Y95V
the isoform CAD4 mutant shows decreased catalytic efficiency compared to the wild type enzyme
additional information
construction of null-mutants of both genes AtCAD-C and AtCAD-D showing highly reduced enzyme activity, but only the latter shows slightly modificated lignin structure, construction of transgenic plants by infection with recombinant Agrobacterium tumefaciens strain C58pMP90 via flower infiltration method, expression pattern of AtCAD-C and AtCAD-D
additional information
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size
additional information
-
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size
additional information
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size, as well as lignin modifications, overview
additional information
-
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size, as well as lignin modifications, overview
additional information
-
in double mutant strain lacking the activities of isoforms cad-4 and cad-5, the material strength properties of the stem plant material are greatly diminished due to severe reductions in macromolecular lignin content. Initially the overall pattern of phenolic deposition in the mutant is very similar to wild-type. Shortly into the stage involving 8-O-4'-linkage formation, deposition is aborted. At this final stage, the double mutant retains a very limited ability to biosynthesize monolignols as evidenced by cleavage and release of ca. 4% of the monolignol-derived moieties relative to the lignin of the wild-type line. In addition, while small amounts of cleavable p-hydroxycinnamaldehyde-derived moieties are released, the overall frequency of monomer cleavable 8-O-4'-inter-unit linkages closely approximates that of wild-type for the equivalent level of lignin deposition
additional information
construction of disruption mutants of genes CADC and CADD of Arabidopsis thaliana resulting in the atypical incorporation of hydroxycinnamaldehydes into lignin. The cadc/cadd-deficient and ferulic acid hydroxylase1 (fah1) cadc/cadd-deficient plants are similar in growth to wild-type plants even though their lignin compositions are drastically altered. In contrast, disruption of CAD in the F5H-overexpressing background results in dwarfism. The dwarfed phenotype observed in these plants does not appear to be related to collapsed xylem, a hallmark of many other lignin-deficient dwarf mutants. Mutant cadc/cadd-deficient and fah1 cadc/cadd-deficient, and cadd-deficient-F5H-overexpressing plants have increased enzyme-catalyzed cell wall digestibility. Phenotypes, overview
additional information
-
construction of disruption mutants of genes CADC and CADD of Arabidopsis thaliana resulting in the atypical incorporation of hydroxycinnamaldehydes into lignin. The cadc/cadd-deficient and ferulic acid hydroxylase1 (fah1) cadc/cadd-deficient plants are similar in growth to wild-type plants even though their lignin compositions are drastically altered. In contrast, disruption of CAD in the F5H-overexpressing background results in dwarfism. The dwarfed phenotype observed in these plants does not appear to be related to collapsed xylem, a hallmark of many other lignin-deficient dwarf mutants. Mutant cadc/cadd-deficient and fah1 cadc/cadd-deficient, and cadd-deficient-F5H-overexpressing plants have increased enzyme-catalyzed cell wall digestibility. Phenotypes, overview
additional information
BdCAD1 targeted silencing via highly specific artificial microRNA, Transgenic growth and developmental phenotype, overview. Downregulation of BdCAD1 is associated with a significant decrease in S units and a slight yet not statistically significant increase in G units, resulting in a reduced S/G ratio in lignin composition
additional information
-
BdCAD1 targeted silencing via highly specific artificial microRNA, Transgenic growth and developmental phenotype, overview. Downregulation of BdCAD1 is associated with a significant decrease in S units and a slight yet not statistically significant increase in G units, resulting in a reduced S/G ratio in lignin composition
additional information
-
screening of a chemically induced population of Brachypodium mutants (Bd21-3 background) for red culm coloration and identification of two mutants, Bd4179 and Bd7591, with mutations in the BdCAD1 gene. The amount of sinapic acid ester-linked to cell walls is measured for in the lignin-related CAD grass mutants. Functional complementation of the Bd4179 mutant with the wild-type BdCAD1 allele restores the wild-type phenotype and lignification. The Bdcad1 alleles are responsible for the reddish-brown phenotype
additional information
-
construction of transgenic antisense plants via infection with Agrobacterium tumefaciens, expressing the gene under control of the CaMV35S promotor, and showing down-regulation of the CAD gene up to 83% reduced expression, but no significant changes in lignin profile, quantiy and composition, in the transgenic trees
additional information
CAD down-regulation does not lead to the accumulation of lignin precursors, evaluated composition and properties of flax fibre from plants with silenced CAD gene. CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting. Even if the overall retting time is not shortened, CAD straw is colonized by microorganisms much quicker, and the pectin degradation enzymes act effectively from the very beginning of the retting. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality
additional information
-
CAD down-regulation does not lead to the accumulation of lignin precursors, evaluated composition and properties of flax fibre from plants with silenced CAD gene. CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting. Even if the overall retting time is not shortened, CAD straw is colonized by microorganisms much quicker, and the pectin degradation enzymes act effectively from the very beginning of the retting. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality
additional information
-
CAD down-regulation does not lead to the accumulation of lignin precursors, evaluated composition and properties of flax fibre from plants with silenced CAD gene. CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting. Even if the overall retting time is not shortened, CAD straw is colonized by microorganisms much quicker, and the pectin degradation enzymes act effectively from the very beginning of the retting. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality
-
additional information
-
identification of Tnt1 retrotransposon insertion cad1-1 and cad1-2 mutants of Medicago truncatula that show reduced lignin autofluorescence under UV microscopy and red coloration in interfascicular fibers, Tnt1 retrotransposon insertion-mutagenized Medicago truncatula plants usually contain 20-50 insertions per plant. The phenotype is caused by insertion of retrotransposons into a gene CAD1. Microarray analysis with RNA isolated from stem internodes of the cad1-1 mutant. NMR analysis indicates that the lignin is derived almost exclusively from coniferaldehyde and sinapaldehyde and is therefore strikingly different from classical lignins, which are derived mainly from coniferyl and sinapyl alcohols. Normal growth under standard conditions in the greenhouse or growth chamber, but dwarfed plants when grown at 30°C. Glycome profiling reveals increased extractability of some xylan and pectin epitopes from the cell walls of the cad1-1 mutant but decreased extractability of others, suggesting that aldehyde-dominant lignin significantly alters cell wall structure
additional information
identification of Tnt1 retrotransposon insertion cad1-1 and cad1-2 mutants of Medicago truncatula that show reduced lignin autofluorescence under UV microscopy and red coloration in interfascicular fibers, Tnt1 retrotransposon insertion-mutagenized Medicago truncatula plants usually contain 20-50 insertions per plant. The phenotype is caused by insertion of retrotransposons into a gene CAD1. Microarray analysis with RNA isolated from stem internodes of the cad1-1 mutant. NMR analysis indicates that the lignin is derived almost exclusively from coniferaldehyde and sinapaldehyde and is therefore strikingly different from classical lignins, which are derived mainly from coniferyl and sinapyl alcohols. Normal growth under standard conditions in the greenhouse or growth chamber, but dwarfed plants when grown at 30°C. Glycome profiling reveals increased extractability of some xylan and pectin epitopes from the cell walls of the cad1-1 mutant but decreased extractability of others, suggesting that aldehyde-dominant lignin significantly alters cell wall structure
additional information
-
structure-based mutagenesis of Mt-CAD2 reveals and confirms the roles of key residues involved in catalysis and substrate binding and affords the engineering of catalytically active variants with increased turnover of sinapaldehyde
additional information
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi displaying normal growth and development and slight effects on lignin production, but the xylem shows an altered content in phenolic lignin forming compounds, metanolic profiling
additional information
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi displaying normal growth and development and slight effects on lignin production, but the xylem shows an altered content in phenolic lignin forming compounds, metanolic profiling
additional information
-
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi displaying normal growth and development and slight effects on lignin production, but the xylem shows an altered content in phenolic lignin forming compounds, metanolic profiling
additional information
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi, transformation using the Agrobacterium tumefaciens system, the transgenic plants display normal growth and development and slight effects on lignin production, but the xylem shows an altered content in lignin forming compounds, metanolic profiling by gas and liquid chromatography mass spectrometry
additional information
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi, transformation using the Agrobacterium tumefaciens system, the transgenic plants display normal growth and development and slight effects on lignin production, but the xylem shows an altered content in lignin forming compounds, metanolic profiling by gas and liquid chromatography mass spectrometry
additional information
-
construction of transgenic tobacco plants with reduced expression of CAD1 by RNAi, transformation using the Agrobacterium tumefaciens system, the transgenic plants display normal growth and development and slight effects on lignin production, but the xylem shows an altered content in lignin forming compounds, metanolic profiling by gas and liquid chromatography mass spectrometry
additional information
-
study in the xylem of tobacco plants in which the expression of cinnamoyl CoA reductase, cinnamyl alcohol dehydrogenase or both are downregulated in order to map the metabolic sphere of influence of the perturbation of lignification. Cinnamyl alcohol dehydrogenase downregulated tobacco is enriched in transcript of light- and cell-wall-related genes and its lignin incorporates more aldehydes. The strain accumulates strongly the substrates of the suppressed enzyme, coniferaldehyde and sinapaldehyde
additional information
-
the GH2-mutant cells are enzyme-inactive and lignin-deficient
additional information
-
down-regulation of CAD expression in callus cultures by RNAi method leads to an reduction of 80% of enzyme activity and the accumulation of dihydroconiferyl alcohol, DHCA
additional information
-
in PhCAD1 the active site residue G302 from the sinapyl alcohol dehydrogenase, SAD, is mutated to C302 and active site residue A293 is mutated to M293. Accumulation of ptox and lignin in PhCAD1-4 isoforms overexpressing transgenic lines, overview
additional information
-
in PhCAD2 the active site residue G302 from the sinapyl alcohol dehydrogenase, SAD, is mutated to A300 and active site residue A293 is mutated to D290
additional information
-
in PhCAD3 the active site residue G302 from the sinapyl alcohol dehydrogenase, SAD, is conserved, but active site residue A293 is mutated to T290. Accumulation of ptox and lignin in PhCAD1-4 isoforms overexpressing transgenic lines, overview
additional information
-
in PhCAD4 the active site residue G302 from the sinapyl alcohol dehydrogenase, SAD, is conserved, but active site residue A293 is mutated to M296
additional information
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-das1 contains an insertion, which results in a truncated protein of 48amino acids. The levels of cad2 mRNA in the midribs of bm1-das1 are reduced by 91%, leading to reductions in total lignin contents by 24%
additional information
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-das1 contains an insertion, which results in a truncated protein of 48amino acids. The levels of cad2 mRNA in the midribs of bm1-das1 are reduced by 91%, leading to reductions in total lignin contents by 24%
additional information
-
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-das1 contains an insertion, which results in a truncated protein of 48amino acids. The levels of cad2 mRNA in the midribs of bm1-das1 are reduced by 91%, leading to reductions in total lignin contents by 24%
additional information
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-ref contains a two-nucleotide insertion in the 3rd exon, which results in a truncated protein of 147 amino acids. The levels of cad2 mRNA in the midribs of bm1-ref are reduced by 86%, leading to reductions in total lignin contents by 30%
additional information
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-ref contains a two-nucleotide insertion in the 3rd exon, which results in a truncated protein of 147 amino acids. The levels of cad2 mRNA in the midribs of bm1-ref are reduced by 86%, leading to reductions in total lignin contents by 30%
additional information
-
maize brown midrib mutant plants, bm1, have reduced lignin content and offer significant advantages when used in silage and biofuel applications. Allele bm1-ref contains a two-nucleotide insertion in the 3rd exon, which results in a truncated protein of 147 amino acids. The levels of cad2 mRNA in the midribs of bm1-ref are reduced by 86%, leading to reductions in total lignin contents by 30%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD1 wild-type in Escherichia coli strain Rosetta2
-
diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD2 wild-type and mutants in Escherichia coli strain Rosetta2
-
entire coding regions of CAD4 cloned into the pET30a vector and expressed in Escherichia coli Rossetta R2 cells
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta cells
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 BdCAD1, DNA and amino acid sequence determination of wild-type and mutant genes, genotyping, phylogenetic analysis and tree, quantitative RT-PCR expression analysis, functional complementation of the cad1 Bd4179 mutant with the wild-type BdCAD1 allele
-
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 CAD, isozyme genotyping, phylogenetic analysis, sequence comparisons, and expression analysis of isozymes
-
gene CAD, phylogenetic analysis and tree
gene CAD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene CAD1, DNA and amino acid sequence determination and analysis, genetic localization CM3.5_scaffold00038, intron-exon structure of melon CAD genes, promoter sequence analysis, phylogenetic analysis, semi-quantitative PCR and quantitative real-time PCR expression analysis
-
gene cad1, DNA and amino acid sequence determination and analysis, MtCAD1 is obtained by reverse genetic screening, genotying, RT-PCR analysis of CAD1 transcripts in cad1-1 and cad1-2 mutant and wild-type lines. The coding sequence of CAD1 driven by the 35S promoter is used for complementation of the cad1-1 mutant. The lignin level in the mutant is significantly restored, and the indene signature disappears, in six independent transformation events. MtCAD1 can also rescue the phenotype of the Arabidopsis thaliana cad4/cad5 double knockout mutant, in which the red coloration in the fibers of the double mutant is no longer visible in the complemented line, and acetyl bromide lignin levels are also partially rescued
gene cad1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD1 in Escherichia coli strain M15
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 CAD2, DNA and amino acid sequence determination and analysis, genetic localization CM3.5_scaffold00034, intron-exon structure of melon CAD genes, promoter sequence analysis, phylogenetic analysis, semi-quantitative PCR and quantitative real time PCR expression analysis
-
gene cad2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene cad2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD1 in Escherichia coli strain M15
gene CAD3, DNA and amino acid sequence determination and analysis, genetic localization CM3.5_scaffold01596, intron-exon structure of melon CAD genes, promoter sequence analysis, phylogenetic analysis, semi-quantitative PCR and quantitative real time PCR expression analysis
-
gene cad3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD3 in Escherichia coli strain M15
gene CAD4, DNA and amino acid sequence determination and analysis, genetic localization CM3.5_scaffold00005, intron-exon structure of melon CAD genes, promoter sequence analysis, phylogenetic analysis, semi-quantitative PCR and quantitative real time PCR expression analysis
-
gene CAD5 or Bradi3g06480, sequence comparisons of the CAD family enzymes from different species, phylogenetic tree
gene CAD5, DNA and amino acid sequence determination and analysis, genetic localization CM3.5_scaffold00059, intron-exon structure of melon CAD genes, promoter sequence analysis, phylogenetic analysis, semi-quantitative PCR and quantitative real time PCR expression analysis
-
gene cad5, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD5 in Escherichia coli strain M15
gene cad7, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD7 in Escherichia coli strain M15
gene cad9, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged PtoCAD9 in Escherichia coli strain M15
gene ctcad1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative realtime PCR enzyme expression analysis
gene ctcad2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative realtime PCR enzyme expression analysis
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
-
gene LtuCAD1, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis, when expressed in the Arabidopsis cad4/cad5 double mutant, LtuCAD1 is able to restore the total lignin content and decrease the S/G lignin ratio, recombinant expressionof the CAD1 gene driven by a CaMV 35S promoter in Arabidopsis thaliana Col-0 using the Agrobacterium tumefaciens strain GV13001 for transfection
gene PaCAD1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PaCAD2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PhCAD1, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis and transcriptome analysis, semi-quantitative RT-PCR enzyme expression analysis, overview. Recombinant expression of His-tagged enzyme
-
gene PhCAD2, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis and transcriptome analysis, semi-quantitative RT-PCR enzyme expression analysis, overview. Recombinant expression of His-tagged enzyme
-
gene PhCAD3, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis and transcriptome analysis, semi-quantitative RT-PCR enzyme expression analysis, overview. Recombinant expression of His-tagged enzyme
-
gene PhCAD4, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis and transcriptome analysis, semi-quantitative RT-PCR enzyme expression analysis, overview. Recombinant expression of His-tagged enzyme
-
gene TaCAD12, cloned from cv. CI12633, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression of GST-tagged enzyme, overexpression of the enyzem and of GFP-tagged enzyme in Triticum aestivum cv. CI12633
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
quantitative realtime PCR enzyme expression analysis during seed development, overview. CAD2 shows the highest expression level of all three CAD isozymes in Carthamus tinctorius
-
-
-
Erianthus sp. IK 76-81
-
1.3 kb cDNA fragment cloned into pGEM-T Easy vector and transformed into competent cell of DH5alpha from Escherichia coli
-
1.3 kb cDNA fragment cloned into pGEM-T Easy vector and transformed into competent cell of DH5alpha from Escherichia coli
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sarni, F.; Grand, C.; Boudet, A.M.
Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana)
Eur. J. Biochem.
139
259-265
1984
Populus x canadensis
brenda
Grima-Pettenati, J.; Chriqui, D.; Sarni-Manchado, P.; Prinsen, E.
Stimulation of lignification in neoformed calli induced by Agrobacterium rhizogenes on bean hypocotyls
Plant Sci.
61
179-188
1989
Vigna mungo
-
brenda
Luderitz, T.; Grisebach, H.
Enzymic synthesis of lignin precursors. Comparison of cinnamoyl-CoA reductase and cinnamyl alcohol:NADP+ dehydrogenase from spruce (Picea abies L.) and soybean (Glycine max L.)
Eur. J. Biochem.
119
115-124
1981
Picea abies
brenda
Wyrambik, D.; Grisebach, H.
Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures
Eur. J. Biochem.
59
9-15
1975
Glycine max
brenda
Kush, A.; Goyvaerts, E.; Chye, M.L.; Chua, N.H.
Laticifer-specific gene expression in Hevea brasiliensis (rubber tree)
Proc. Natl. Acad. Sci. USA
87
1787-1790
1990
Hevea brasiliensis
brenda
Walter, M.H.; Grima-Pettenati, J.; Grand, C.; Boudet, A.M.; Lamb, C.J.
Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis: cDNA cloning and mRNA induction by fungal elicitor
Proc. Natl. Acad. Sci. USA
85
5546-5550
1988
Phaseolus vulgaris
brenda
Grand, C.; Sarni, F.; Lamb, C.J.
Rapid induction by fungal elicitor of the synthesis of cinnamyl-alcohol dehydrogenase, a specific enzyme of lignin synthesis
Eur. J. Biochem.
169
73-77
1987
Phaseolus vulgaris
brenda
Moerschbacher, B.; Heck, B.; Kogel, K.H.; Obst, O.; Reisener, H.J.
An elicitor of the hypersensitive lignification response in wheat leaves isolated from the rust fungus Puccinia graminis f. sp. tritici H. Induction of enzymes correlated with the biosynthesis of lignin
Z. Naturforsch. C
41
839-844
1986
Triticum aestivum
-
brenda
Kutsuki, H.; Shimada, M.; Higuchi, T.
Regulatory role of cinnamyl alcohol dehydrogenase in the formation of guaiacyl and syringyl lignins
Phytochemistry
21
19-23
1982
Cryptomeria japonica, Erythrina crista-galli, Ginkgo biloba, Liriodendron tulipifera, Metasequoia glyptostroboides, Pinus thunbergii, Platycladus orientalis, Populus x canadensis, Prunus persica, Prunus yedoensis, Robinia pseudoacacia
-
brenda
Kutsuki, H.; Higuchi, T.
Activities of some enzymes of lignin formation in reaction wood of Thuja orientalis, Metasequoia glyptostroboides and Robinia pseudoacacia
Planta
152
365-368
1981
Metasequoia glyptostroboides, Robinia pseudoacacia, Platycladus orientalis
brenda
Mansell, R.L.; Gross, G.G.; Stckigt, J.; Franke, H.; Zenk, M.H.
Purification and properties of cinnamyl alcohol dehydrogenase from higher plants involved in lignin biosynthesis
Phytochemistry
13
2427-2435
1974
Abies nobilis, Acer campestre, Acer saccharinum, Athyrium filix-femina, Atrichum undulatum, Avena sativa, Betula pendula, Cichorium endivia, Cormus domestica, Corylus sp., Daucus carota, Equisetum arvense, Equisetum palustre, Forsythia suspensa, Ginkgo biloba, Helianthus annuus, Heracleum mantegazzianum, Hordeum sp., Ilex aquifolium, Larix kaempferi, Ligustrum vulgare, Linum usitatissimum, Liriodendron tulipifera, Metasequoia glyptostroboides, Morinda citrifolia, Nephrolepis exaltata, Picea abies, Pinus peuce, Pinus strobus, Pisum sativum, Platanus x hispanica, Populus nigra, Populus tremula, Prunus serotina, Pseudotsuga menziesii, Pteris cretica, Pteris wimsetti, Quercus robur, Quercus rubra, Salix alba, Salvinia natans, Sambucus racemosa, Secale cereale, Selaginella kraussiana, Selaginella martensii, Sorbus aucuparia, Sphagnum sp., Syringa vulgaris, Taxus baccata, Thuja plicata, Woodwardia radicans, Zea mays
-
brenda
Wyrambik, D.; Grisebach, H.
Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures
Eur. J. Biochem.
97
503-509
1979
Glycine max
brenda
Klischies, M.; Stckigt, J.; Zenk, M.H.
Stereospecificity of cinnamoyl alcohol dehydrogenase and synthesis of stereospecifically labelled coniferyl alcohol
Phytochemistry
17
1523-1525
1978
Forsythia suspensa
-
brenda
McKie, J.H.; Jaouhari, R.; Douglas, K.T.; Goffner, D.; Feuillet, C.; Grima-Pettenati, J.; Boudet, A.M.; Baltas, M.; Gorrichon, L.
A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification
Biochim. Biophys. Acta
1202
61-69
1993
Eucalyptus sp.
brenda
Lauvergeat, V.; Kennedy, K.; Feuillet, C.; McKie, J.H.; Gorrichon, L.; Baltas, M.; Boudet, A.M.; Grima-Pettenati, J.; Douglas, K.T.
Site-directed mutagenesis of a serine residue in cinnamyl alcohol dehydrogenase, a plant NADPH-dependent dehydrogenase, affects the specificity for the coenzyme
Biochemistry
34
12426-12434
1995
Eucalyptus gunnii
brenda
Logemann, E.; Reinold, S.; Somssich, I.E.; Hahlbrock, K.
A novel type of pathogen defense-related cinnamyl alcohol dehydrogenase
Biol. Chem.
378
909-913
1997
Petroselinum crispum
brenda
Nakashima, J.; Awano, T.; Takabe, K.; Fujita, M.; Saiki, H.
Immunocytochemical localization of phenylalanine ammonia-lyase and cinnamyl alcohol dehydrogenase in differentiating tracheary elements derived from Zinnia mesophyll cells
Plant Cell Physiol.
38
113-123
1997
Zinnia elegans
-
brenda
O'Malley, D.M.; Porter, S.; Sederoff, R.R.
Purification, characterization, and cloning of cinnamyl alcohol dehydrogenase in loblolly pine (Pinus taeda L.)
Plant Physiol.
98
1364-1371
1992
Pinus taeda
brenda
Hibino, T.; Shibata, D.; Umezawa, T.; Higuchi, T.
Purification and partial sequences of Aralia cordata cinnamyl alcohol dehydrogenase
Phytochemistry
32
565-567
1993
Aralia cordata
brenda
Mitchell, H.J.; Hall, S.A.; Stratford, R.; Hall, J.L.; Barber, M.S.
Differential induction of cinnamyl alcohol dehydrogenase during defensive lignification in wheat (Triticum aestivum). Characterization of the major inducible form
Planta
208
31-37
1999
Triticum aestivum
-
brenda
Grima-Pettenati, J.; Campargue, C.; Boudet, A.; Boudet, A.M.
Purification and characterization of cinnamyl alcohol dehydrogenase isoforms from Phaseolus vulgaris
Phytochemistry
37
941-947
1994
Phaseolus vulgaris
brenda
Samaj, J.; Hawkins, S.; Lauvergeat, V.; Grima-Pettenati, J.; Boudet, A.
Immunolocalization of cinnamyl alcohol dehydrogenase 2 (CAD 2) indicates a good correlation with cell-specific activity of CAD 2 promoter in transgenic poplar shoots
Planta
204
437-443
1998
Populus tremula x Populus alba
brenda
Goffner, D.; Van Doorsselaere, J.; Yahiaoui, N.; Samaj, J.; Grima-Pettenati, J.; Boudet, A.M.
A novel aromatic alcohol dehydrogenase in higher plants: molecular cloning and expression
Plant Mol. Biol.
36
755-765
1998
Eucalyptus gunnii
brenda
Blanco-Portales, R.; Medina-Escobar, N.; Lopez-Raez, J.A.; Gonzalez-Reyes, J.A.; Villalba, J.M.; Moyano, E.; Caballero, J.L.; Munoz-Blanco, J.
Cloning, expression and immunolocalization pattern of a cinnamyl alcohol dehydrogenase gene from strawberry (Fragaria x ananassa cv. Chandler)
J. Exp. Bot.
53
1723-1734
2002
Fragaria x ananassa (Q9ATW1), Fragaria x ananassa
brenda
Valencia, E.; Larroy, C.; Ochoa, W.F.; Pares, X.; Fita, I.; Biosca, J.A.
Apo and Holo structures of an NADP(H)-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae
J. Mol. Biol.
341
1049-1062
2004
Saccharomyces cerevisiae
brenda
Valerio, L.; Carter, D.; Rodrigues, J.C.; Tournier, V.; Gominho, J.; Marque, C.; Boudet, A.M.; Maunders, M.; Pereira, H.; Teulieres, C.
Down regulation of cinnamyl alcohol dehydrogenase, a lignification enzyme, in Eucalyptus camaldulensis
Mol. Breed.
12
157-167
2003
Eucalyptus camaldulensis
brenda
Ruelland, E.; Campalans, A.; Selman-Housein, G.; Puigdomenech, P.; Rigau, J.
Cellular and subcellular localization of the lignin biosynthetic enzymes caffeic acid-O-methyltransferase, cinnamyl alcohol dehydrogenase and cinnamoyl-coenzyme A reductase in two monocots, sugarcane and maize
Physiol. Plant.
117
93-99
2003
Saccharum officinarum
-
brenda
Sibout, R.; Eudes, A.; Pollet, B.; Goujon, T.; Mila, I.; Granier, F.; Seguin, A.; Lapierre, C.; Jouanin, L.
Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants
Plant Physiol.
132
848-860
2003
Arabidopsis thaliana (Q02971)
brenda
Mee, B.; Kelleher, D.; Frias, J.; Malone, R.; Tipton, K.F.; Henehan, G.T.; Windle, H.J.
Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori. An aldehyde dismutating enzyme
FEBS J.
272
1255-1264
2005
Helicobacter pylori
brenda
Youn, B.; Camacho, R.; Moinuddin, S.G.; Lee, C.; Davin, L.B.; Lewis, N.G.; Kang, C.
Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4
Org. Biomol. Chem.
4
1687-1697
2006
Arabidopsis thaliana (O49482), Arabidopsis thaliana (P48523), Arabidopsis thaliana
brenda
Sibout, R.; Eudes, A.; Mouille, G.; Pollet, B.; Lapierre, C.; Jouanin, L.; Seguin, A.
Cinnamyl alcohol dehydrogenase-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis
Plant Cell
17
2059-2076
2005
Arabidopsis thaliana (P48523), Arabidopsis thaliana
brenda
Damiani, I.; Morreel, K.; Danoun, S.; Goeminne, G.; Yahiaoui, N.; Marque, C.; Kopka, J.; Messens, E.; Goffner, D.; Boerjan, W.; Boudet, A.M.; Rochange, S.
Metabolite profiling reveals a role for atypical cinnamyl alcohol dehydrogenase CAD1 in the synthesis of coniferyl alcohol in tobacco xylem
Plant Mol. Biol.
59
753-769
2005
Nicotiana tabacum (Q5D4P8), Nicotiana tabacum (Q5D4P9), Nicotiana tabacum
brenda
Zhang, K.; Qian, Q.; Huang, Z.; Wang, Y.; Li, M.; Hong, L.; Zeng, D.; Gu, M.; Chu, C.; Cheng, Z.
Gold-hull-and-internode2-gene encodes a primarily multifunctional cinnamyl-alcohol dehydrogenase in rice
Plant Physiol.
140
972-983
2006
Oryza sativa
brenda
Moeller, R.; Steward, D.; Phillips, L.; Flint, H.; Wagner, A.
Gene silencing of cinnamyl alcohol dehydrogenase in Pinus radiata callus cultures
Plant Physiol. Biochem.
43
1061-1066
2005
Pinus radiata
brenda
Ali, M.B.; Hahn, E.J.; Paek, K.Y.
CO2-induced total phenolics in suspension cultures of Panax ginseng C.A. Mayer roots: role of antioxidants and enzymes
Plant Physiol. Biochem.
43
449-457
2005
Panax ginseng
brenda
Ali, M.B.; Singh, N.; Shohael, A.M.; Hahn, E.J.; Paek, K.
Phenolics metabolism and lignin synthesis in root suspension cultures of Panax ginseng in response to copper stress
Plant Sci.
171
147-154
2006
Panax ginseng
brenda
Hano, C.; Addi, M.; Bensaddek, L.; Cronier, D.; Baltora-Rosset, S.; Doussot, J.; Maury, S.; Mesnard, F.; Chabbert, B.; Hawkins, S.; Laine, E.; Lamblin, F.
Differential accumulation of monolignol-derived compounds in elicited flax (Linum usitatissimum) cell suspension cultures
Planta
223
975-989
2006
Linum usitatissimum (Q1HGA8), Linum usitatissimum
brenda
Eudes, A.; Pollet, B.; Sibout, R.; Do, C.T.; Seguin, A.; Lapierre, C.; Jouanin, L.
Evidence for a role of AtCAD 1 in lignification of elongating stems of Arabidopsis thaliana
Planta
225
23-39
2006
Arabidopsis thaliana (Q02971), Arabidopsis thaliana
brenda
Moeller, R.; Koch, G.; Nanayakkara, B.; Schmitt, U.
Lignification in cell cultures of Pinus radiata: activities of enzymes and lignin topochemistry
Tree Physiol.
26
201-210
2006
Pinus radiata
brenda
Tsuruta, S.; Ebina, M.; Nakagawa, H.; Kawamura, O.; Akashi, R.
Isolation and characterization of cDNA encoding cinnamyl alcohol dehydrogenase (CAD) in sorghum (Sorghum bicolor (L.) Moench)
Grassl. Sci.
53
103-109
2007
Sorghum bicolor (A1ILL4)
-
brenda
Chen, A.P.; Zhong, N.Q.; Qu, Z.L.; Wang, F.; Liu, N.; Xia, G.X.
Root and vascular tissue-specific expression of glycine-rich protein AtGRP9 and its interaction with AtCAD5, a cinnamyl alcohol dehydrogenase, in Arabidopsis thaliana
J. Plant Res.
120
337-343
2007
Arabidopsis thaliana
brenda
Luo, Z.; Xu, X.; Yan, B.
Use of 1-methylcyclopropene for alleviating chilling injury and lignification of bamboo shoot (Phyllostachys praecox f. prevernalis) during cold storage
J. Sci. Food Agric.
88
151-157
2008
Phyllostachys praecox
brenda
Ali, M.B.; Hahn, E.; Paek, K.
Methyl jasmonate and salicylic acid induced oxidative stress and accumulation of phenolics in Panax ginseng bioreactor root suspension cultures
Molecules
12
607-621
2007
Panax ginseng
brenda
Jourdes, M.; Cardenas, C.L.; Laskar, D.D.; Moinuddin, S.G.; Davin, L.B.; Lewis, N.G.
Plant cell walls are enfeebled when attempting to preserve native lignin configuration with poly-p-hydroxycinnamaldehydes: evolutionary implications
Phytochemistry
68
1932-1956
2007
Arabidopsis thaliana
brenda
Kim, S.J.; Kim, K.W.; Cho, M.H.; Franceschi, V.R.; Davin, L.B.; Lewis, N.G.
Expression of cinnamyl alcohol dehydrogenases and their putative homologues during Arabidopsis thaliana growth and development: lessons for database annotations?
Phytochemistry
68
1957-1974
2007
Arabidopsis thaliana
brenda
Prats, E.; Martinez, F.; Rojas-Molina, M.M.; Rubiales, D.
Differential effects of phenylalanine ammonia lyase, cinnamyl alcohol dehydrogenase, and energetic metabolism inhibition on resistance of appropriate host and nonhost cereal-rust interactions
Phytopathology
97
1578-1583
2007
Hordeum vulgare, Triticum aestivum
brenda
Dauwe, R.; Morreel, K.; Goeminne, G.; Gielen, B.; Rohde, A.; Van Beeumen, J.; Ralph, J.; Boudet, A.M.; Kopka, J.; Rochange, S.F.; Halpin, C.; Messens, E.; Boerjan, W.
Molecular phenotyping of lignin-modified tobacco reveals associated changes in cell-wall metabolism, primary metabolism, stress metabolism and photorespiration
Plant J.
52
263-285
2007
Nicotiana tabacum
brenda
Zucca, P.; Littarru, M.; Rescigno, A.; Sanjust, E.
Cofactor recycling for selective enzymatic biotransformation of cinnamaldehyde to cinnamyl alcohol
Biosci. Biotechnol. Biochem.
73
1224-1226
2009
Saccharomyces cerevisiae
brenda
Barakat, A.; Bagniewska-Zadworna, A.; Choi, A.; Plakkat, U.; DiLoreto, D.S.; Yellanki, P.; Carlson, J.E.
The cinnamyl alcohol dehydrogenase gene family in Populus: phylogeny, organization, and expression
BMC Plant Biol.
9
26
2009
Populus trichocarpa
brenda
Vidal, R.; Lopez-Maury, L.; Guerrero, M.G.; Florencio, F.J.
Characterization of an alcohol dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803 that responds to environmental stress conditions via the Hik34-Rre1 two-component system
J. Bacteriol.
191
4383-4391
2009
Synechocystis sp.
brenda
Nur Fariza, M.; Pang, S.; Choong, C.; Wickneswari, R.
Extensive DNA sequence variations in two lignin genes, Cinnamate 4-hydroxylase and Cinnamyl Alcohol Dehydrogenase from Acacia mangium and Acacia auriculiformis
J. Biol. Sci.
8
687-690
2008
Acacia mangium, Acacia auriculiformis
-
brenda
Bhuiyan, N.H.; Selvaraj, G.; Wei, Y.; King, J.
Gene expression profiling and silencing reveal that monolignol biosynthesis plays a critical role in penetration defence in wheat against powdery mildew invasion
J. Exp. Bot.
60
509-521
2009
Triticum monococcum
brenda
Kovacik, J.; Klejdus, B.; Backor, M.
Phenolic metabolism of Matricaria chamomilla plants exposed to nickel
J. Plant Physiol.
166
1460-1464
2009
Matricaria chamomilla
brenda
Bedon, F.; Levasseur, C.; Grima-Pettenati, J.; Seguin, A.; MacKay, J.
Sequence analysis and functional characterization of the promoter of the Picea glauca cinnamyl alcohol dehydrogenase gene in transgenic white spruce plants
Plant Cell Rep.
28
787-800
2009
Pinus taeda, Picea glauca (B7U3W7), Picea glauca
brenda
Li, X.; Yang, Y.; Yao, J.; Chen, G.; Li, X.; Zhang, Q.; Wu, C.
FLEXIBLE CULM 1 encoding a cinnamyl-alcohol dehydrogenase controls culm mechanical strength in rice
Plant Mol. Biol.
69
685-697
2009
Oryza sativa Japonica Group (Q0JA75)
brenda
Sattler, S.E.; Saathoff, A.J.; Haas, E.J.; Palmer, N.A.; Funnell-Harris, D.L.; Sarath, G.; Pedersen, J.F.
A nonsense mutation in a cinnamyl alcohol dehydrogenase gene is responsible for the Sorghum brown midrib6 phenotype
Plant Physiol.
150
584-595
2009
Sorghum bicolor, Sorghum bicolor (A1ILL4), Sorghum bicolor (C5XC49)
brenda
Saidi, I.; Ammar, S.; Demont-Caulet, N.; Thevenin, J.; Lapierre, C.; Bouzid, S.; Jouanin, L.
Thigmomorphogenesis in Solanum lycopersicum: Morphological and biochemical responses in stem after mechanical stimulation
Plant Sci.
177
1-6
2009
Solanum lycopersicum
brenda
Ma, Q.H.
Functional analysis of a cinnamyl alcohol dehydrogenase involved in lignin biosynthesis in wheat
J. Exp. Bot.
61
2735-2744
2010
Triticum aestivum (D7PGW0), Triticum aestivum
brenda
Kim, Y.H.; Bae, J.M.; Huh, G.H.
Transcriptional regulation of the cinnamyl alcohol dehydrogenase gene from sweetpotato in response to plant developmental stage and environmental stress
Plant Cell Rep.
29
779-791
2010
Ipomoea batatas, Ipomoea batatas cv. Yulmi
brenda
Pennacchio, A.; Rossi, M.; Raia, C.A.
Synthesis of cinnamyl alcohol from cinnamaldehyde with Bacillus stearothermophilus alcohol dehydrogenase as the isolated enzyme and in recombinant E. coli cells
Appl. Biochem. Biotechnol.
170
1482-1490
2013
Geobacillus stearothermophilus
brenda
Saathoff, A.; Tobias, C.; Sattler, S.; Haas, E.; Twigg, P.; Sarath, G.
Switchgrass contains two cinnamyl alcohol dehydrogenases involved in lignin formation
Bioenergy Res.
4
120-133
2011
Panicum virgatum (E2DIF4), Panicum virgatum (E2DIF5)
-
brenda
Nishimura, M.; Kohno, K.; Nishimura, Y.; Inagaki, M.; Davies, J.
Characterization of two isozymes of coniferyl alcohol dehydrogenase from Streptomyces sp. NL15-2K
Biosci. Biotechnol. Biochem.
75
1770-1777
2011
Streptomyces sp.
brenda
Seo, K.H.; Zhuang, N.; Chen, C.; Song, J.Y.; Kang, H.L.; Rhee, K.H.; Lee, K.H.
Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis
FEBS Lett.
586
337-343
2012
Helicobacter pylori (D0ITF8), Helicobacter pylori
brenda
Deng, W.W.; Zhang, M.; Wu, J.Q.; Jiang, Z.Z.; Tang, L.; Li, Y.Y.; Wei, C.L.; Jiang, C.J.; Wan, X.C.
Molecular cloning, functional analysis of three cinnamyl alcohol dehydrogenase (CAD) genes in the leaves of tea plant, Camellia sinensis
J. Plant Physiol.
170
272-282
2013
Camellia sinensis (F6L7F4), Camellia sinensis (F6L7F5), Camellia sinensis (G4VV62), Camellia sinensis
brenda
Cheng, H.; Li, L.; Xu, F.; Cheng, S.; Cao, F.; Wang, Y.; Yuan, H.; Jiang, D.; Wu, C.
Expression patterns of a cinnamyl alcohol dehydrogenase gene involved in lignin biosynthesis and environmental stress in Ginkgo biloba
Mol. Biol. Rep.
40
707-721
2013
Ginkgo biloba (E5F5P7), Ginkgo biloba
brenda
Fornale, S.; Capellades, M.; Encina, A.; Wang, K.; Irar, S.; Lapierre, C.; Ruel, K.; Joseleau, J.P.; Berenguer, J.; Puigdomenech, P.; Rigau, J.; Caparros-Ruiz, D.
Altered lignin biosynthesis improves cellulosic bioethanol production in transgenic maize plants down-regulated for cinnamyl alcohol dehydrogenase
Mol. Plant
5
817-830
2012
Zea mays
brenda
Lee, C.; Bedgar, D.L.; Davin, L.B.; Lewis, N.G.
Assessment of a putative proton relay in Arabidopsis cinnamyl alcohol dehydrogenase catalysis
Org. Biomol. Chem.
11
1127-1134
2013
Arabidopsis thaliana (O49482), Arabidopsis thaliana
brenda
Santiago, R.; Alarcon, B.; de Armas, R.; Vicente, C.; Legaz, M.E.
Changes in cinnamyl alcohol dehydrogenase activities from sugarcane cultivars inoculated with Sporisorium scitamineum sporidia
Physiol. Plant.
145
245-259
2012
Saccharum sp., Saccharum sp. B42231, Saccharum sp. My 5514
brenda
Chen, W.; VanOpdorp, N.; Fitzl, D.; Tewari, J.; Friedemann, P.; Greene, T.; Thompson, S.; Kumpatla, S.; Zheng, P.
Transposon insertion in a cinnamyl alcohol dehydrogenase gene is responsible for a brown midrib1 mutation in maize
Plant Mol. Biol.
80
289-297
2012
Zea mays (B6U7D8), Zea mays (J7FTC5), Zea mays
brenda
Pandey, B.; Pandey, V.P.; Dwivedi, U.N.
Cloning, expression, functional validation and modeling of cinnamyl alcohol dehydrogenase isolated from xylem of Leucaena leucocephala
Protein Expr. Purif.
79
197-203
2011
Leucaena leucocephala (B5TR18), Leucaena leucocephala
brenda
Trabucco, G.M.; Matos, D.A.; Lee, S.J.; Saathoff, A.J.; Priest, H.D.; Mockler, T.C.; Sarath, G.; Hazen, S.P.
Functional characterization of cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase in Brachypodium distachyon
BMC Biotechnol.
13
61
2013
Brachypodium distachyon (I1HY48), Brachypodium distachyon
brenda
Rong, W.; Luo, M.; Shan, T.; Wei, X.; Du, L.; Xu, H.; Zhang, Z.
A wheat cinnamyl alcohol dehydrogenase TaCAD12 contributes to host resistance to the sharp eyespot disease
Front. Plant Sci.
7
1723
2016
Triticum aestivum, Triticum aestivum (A0A1D6BJ11)
brenda
Bhattacharyya, D.; Hazra, S.; Banerjee, A.; Datta, R.; Kumar, D.; Chakrabarti, S.; Chattopadhyay, S.
Transcriptome-wide identification and characterization of CAD isoforms specific for podophyllotoxin biosynthesis from Podophyllum hexandrum
Plant Mol. Biol.
92
1-23
2016
Sinopodophyllum hexandrum
brenda
Sun, Y.; Wu, Y.; Zhao, Y.; Han, X.; Lou, H.; Cheng, A.
Molecular cloning and biochemical characterization of two cinnamyl alcohol dehydrogenases from a liverwort Plagiochasma appendiculatum
Plant Physiol. Biochem.
70
133-141
2013
Plagiochasma appendiculatum, Plagiochasma appendiculatum (T1SEU9), Plagiochasma appendiculatum (T1SEV0)
brenda
Zhao, Q.; Tobimatsu, Y.; Zhou, R.; Pattathil, S.; Gallego-Giraldo, L.; Fu, C.; Jackson, L.A.; Hahn, M.G.; Kim, H.; Chen, F.; Ralph, J.; Dixon, R.A.
Loss of function of cinnamyl alcohol dehydrogenase 1 leads to unconventional lignin and a temperature-sensitive growth defect in Medicago truncatula
Proc. Natl. Acad. Sci. USA
110
13660-13665
2013
Medicago truncatula, Medicago truncatula (A0A072UJB3)
brenda
Pandey, B.; Pandey, V.P.; Shasany, A.K.; Dwivedi, U.N.
Purification and characterization of a zinc-dependent cinnamyl alcohol dehydrogenase from Leucaena leucocephala, a tree legume
Appl. Biochem. Biotechnol.
172
3414-3423
2014
Leucaena leucocephala
brenda
Choi, B.; Chung, J.; Bae, H.; Bae, I.; Park, S.; Bae, H.
Functional characterization of cinnamyl alcohol dehydrogenase during developmental stages and under various stress conditions in kenaf (Hibiscus cannabinus L.)
BioResources
11
105-125
2016
Hibiscus cannabinus (A0A0U1ZF25), Hibiscus cannabinus (D9ZKR7)
-
brenda
Preisner, M.; Kulma, A.; Zebrowski, J.; Dyminska, L.; Hanuza, J.; Arendt, M.; Starzycki, M.; Szopa, J.
Manipulating cinnamyl alcohol dehydrogenase (CAD) expression in flax affects fibre composition and properties
BMC Plant Biol.
14
50
2014
Linum usitatissimum (Q1HGA8), Linum usitatissimum, Linum usitatissimum Nike (Q1HGA8)
brenda
Patel, P.; Gupta, N.; Gaikwad, S.; Agrawal, D.C.; Khan, B.M.
Leucaena sp. recombinant cinnamyl alcohol dehydrogenase: purification and physicochemical characterization
Int. J. Biol. Macromol.
63
254-260
2014
Leucaena leucocephala (B5AR58), Leucaena leucocephala
brenda
Gabotti, D.; Negrini, N.; Morgutti, S.; Nocito, F.F.; Cocucci, M.
Cinnamyl alcohol dehydrogenases in the mesocarp of ripening fruit of Prunus persica genotypes with different flesh characteristics: changes in activity and protein and transcript levels
Physiol. Plant.
154
329-348
2015
Prunus persica
brenda
Ragamustari, S.; Shiraiwa, N.; Hattori, T.; Nakatsubo, T.; Suzuki, S.; Umezawa, T.
Characterization of three cinnamyl alcohol dehydrogenases from Carthamus tinctorius
Plant Biotechnol.
30
315-326
2013
Carthamus tinctorius (U3TDQ6), Carthamus tinctorius (U3TH11), Carthamus tinctorius (U3TI46)
-
brenda
Pan, H.; Zhou, R.; Louie, G.V.; Muehlemann, J.K.; Bomati, E.K.; Bowman, M.E.; Dudareva, N.; Dixon, R.A.; Noel, J.P.; Wang, X.
Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis
Plant Cell
26
3709-3727
2014
Medicago truncatula
brenda
Anderson, N.A.; Tobimatsu, Y.; Ciesielski, P.N.; Ximenes, E.; Ralph, J.; Donohoe, B.S.; Ladisch, M.; Chapple, C.
Manipulation of guaiacyl and syringyl monomer biosynthesis in an Arabidopsis cinnamyl alcohol dehydrogenase mutant results in atypical lignin biosynthesis and modified cell wall structure
Plant Cell
27
2195-2209
2015
Arabidopsis thaliana (P48523), Arabidopsis thaliana
brenda
Bouvier D'Yvoire, M.; Bouchabke-Coussa, O.; Voorend, W.; Antelme, S.; Cezard, L.; Legee, F.; Lebris, P.; Legay, S.; Whitehead, C.; McQueen-Mason, S.; Gomez, L.; Jouanin, L.; Lapierre, C.; Sibout, R.
Disrupting the cinnamyl alcohol dehydrogenase 1 gene (BdCAD1) leads to altered lignification and improved saccharification in Brachypodium distachyon
Plant J.
73
496-508
2013
Brachypodium distachyon
brenda
Xu, Y.; Thammannagowda, S.; Thomas, T.; Azadi, P.; Schlarbaum, S.; Liang, H.
LtuCAD1 is a cinnamyl alcohol dehydrogenase ortholog involved in lignin biosynthesis in Liriodendron tulipifera L., a basal angiosperm timber species
Plant Mol. Biol. Rep.
31
1089-1099
2013
Liriodendron tulipifera (G3DSC5)
brenda
Chao, N.; Liu, S.X.; Liu, B.M.; Li, N.; Jiang, X.N.; Gai, Y.
Molecular cloning and functional analysis of nine cinnamyl alcohol dehydrogenase family members in c
Planta
240
1097-1112
2014
Populus tomentosa (A0A023RBJ1), Populus tomentosa (KJ159967), Populus tomentosa (T1WUT6), Populus tomentosa (T1WUU2), Populus tomentosa (T1WVG5), Populus tomentosa (T1WW77), Populus tomentosa (T1WW82), Populus tomentosa (T1WWB9), Populus tomentosa (T1WWR8), Populus tomentosa
brenda
Jin, Y.; Zhang, C.; Liu, W.; Qi, H.; Chen, H.; Cao, S.
The cinnamyl alcohol dehydrogenase gene family in melon (Cucumis melo L.): bioinformatic analysis and expression patterns
PLoS ONE
9
e101730
2014
Cucumis melo
brenda
Kasirajan, L.; Valiyaparambth, R.; Kubandiran, A.; Velu, J.
Isolation, cloning and expression analysis of cinnamyl alcohol dehydrogenase (CAD) involved in phenylpropanoid pathway of Erianthus arundinaceus, a wild relative of sugarcane
3 Biotech
10
11
2019
Erianthus sp. IK 76-81
brenda
Wenmin, Q.; Xixi, S.; Xiaojiao, H.; Mingying, L.; Guirong, Q.; Renying, Z.
Overexpression of Sedum alfredii cinnamyl alcohol dehydrogenase increases the tolerance and accumulation of cadmium in Arabidopsis
Environ. Exp. Bot.
155
566-577
2018
Sedum alfredii
-
brenda
Dorairaj, D.; Ismail, M.R.
Distribution of silicified microstructures, regulation of cinnamyl alcohol dehydrogenase and lodging resistance in silicon and paclobutrazol mediated Oryza sativa
Front. Physiol.
8
491
2017
Oryza sativa Japonica Group (A0A0P0VFU1)
brenda
Dongming, M.; Chong, X.; Fatima, A.-G.; Hong, W.; Jinfen, Y.; Rika, J.; De-Yu, X.
Overexpression of Artemisia annua cinnamyl alcohol dehydrogenase increases lignin and coumarin and reduces artemisinin and other sesquiterpenes
Front. Plant Sci.
9
828
2018
Artemisia annua (A0A2Z5D8A5), Artemisia annua
brenda
Preisner, M.; Wojtasik, W.; Kostyn, K.; Boba, A.; Czuj, T.; Szopa, J.; Kulma, A.
The cinnamyl alcohol dehydrogenase family in flax Differentiation during plant growth and under stress conditions
J. Plant Physiol.
221
132-143
2018
Linum usitatissimum (Q1HGA8), Linum usitatissimum
brenda
Park, H.L.; Kim, T.L.; Bhoo, S.H.; Lee, T.H.; Lee, S.W.; Cho, M.H.
Biochemical characterization of the rice cinnamyl alcohol dehydrogenase gene family
Molecules
23
2659
2018
Oryza sativa Japonica Group (Q0JA75), Oryza sativa Japonica Group (Q6ZHS4), Oryza sativa Japonica Group (Q7XWU3)
brenda
Liu, X.; Van Acker, R.; Voorend, W.; Pallidis, A.; Goeminne, G.; Pollier, J.; Morreel, K.; Kim, H.; Muylle, H.; Bosio, M.; Ralph, J.; Vanholme, R.; Boerjan, W.
Rewired phenolic metabolism and improved saccharification efficiency of a Zea mays cinnamyl alcohol dehydrogenase 2 (zmcad2) mutant
Plant J.
105
1240-1257
2021
Zea mays
brenda
Oezparpucu, M.; Rueggeberg, M.; Gierlinger, N.; Cesarino, I.; Vanholme, R.; Boerjan, W.; Burgert, I.
Unravelling the impact of lignin on cell wall mechanics a comprehensive study on young poplar trees downregulated for cinnamyl alcohol dehydrogenase (CAD)
Plant J.
91
480-490
2017
Populus tremula x Populus alba
brenda
Jun, S.Y.; Walker, A.M.; Kim, H.; Ralph, J.; Vermerris, W.; Sattler, S.E.; Kang, C.
The enzyme activity and substrate specificity of two major cinnamyl alcohol dehydrogenases in sorghum (Sorghum bicolor), SbCAD2 and SbCAD4
Plant Physiol.
174
2128-2145
2017
Sorghum bicolor (A1ILL4), Sorghum bicolor (C5XC49)
brenda