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Information on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.195
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.195 cinnamyl-alcohol dehydrogenase
IUBMB Comments
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.195
- lignin
-
lignification
- monolignols
-
phenylpropanoids
-
sinapyl
- xylem
-
coniferyl
-
ammonia-lyase
- cinnamoyl-coa
-
caffeic
- coniferaldehyde
-
guaiacyl
- sinapaldehyde
- eucalyptus
-
cinnamoyl
-
hydroxycinnamyl
-
linum
- taeda
-
p-coumaryl
- cinnamaldehydes
-
syringyl
-
loblolly
- biofuel production
- nutrition
- industry
- biotechnology
-
4-coumarate-coa
-
4.3.1.5
- synthesis
-
thioacidolysis
- 4-coumarate
-
3-o-methyltransferase
- podophyllotoxin
- agriculture
- gunnii
showSynonyms
cinnamyl alcohol dehydrogenase, cad11, cinnamyl-alcohol dehydrogenase, cinnamyl alcohol dehydrogenases, scadh6p, atcad4, tacad12, ptocad1, cinnamyl alcohol dehydrogenase 2, cad10, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BdCAD1
Brown-midrib 1 protein
-
-
-
-
CAD
CAD 7/8
-
-
-
-
CAD1
CAD12
CAD2
CAD3
CAD4
CAD5
CAD6
CAD7
CAD8
CAD9
cinnamyl alcohol dehydrogenase
cinnamyl alcohol dehydrogenase 1
cinnamyl alcohol dehydrogenase 2
dehydrogenase, cinnamyl alcohol
-
-
-
-
additional information
the enzyme belongs to the CAD protein family
CAD
-
-
-
-
CAD
-
CAD2
-
-
-
-
cinnamyl alcohol dehydrogenase
-
-
-
-
cinnamyl alcohol dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
A-specific enzyme
-
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
acts stereospecifically on the pro-R-hydrogen atom of coniferyl alcohol
-
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
-
-
-
-
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
active site structure
-
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
catalytic reaction mechanism, substrate and cofactor binding structure
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
random mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
capsiconiate biosynthesis, phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
cinnamyl-alcohol:NADP+ oxidoreductase
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
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CAS REGISTRY NUMBER
COMMENTARY
55467-36-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dimethylcinnamyl alcohol + NADP+
2,4-dimethylcinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
2-propanol + NADP+
? + NADPH + H+
-
Substrates: 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
Products: -
Products: -
?
3,4-methylenedioxycinnamyl alcohol + NADP+
3,4-methylenedioxycinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
3-methoxybenzylalcohol + NADP+
3-methoxybenzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
3-phenyl-1-propanol + NAD+
3-phenylpropanal + NADH + H+
-
Substrates: -
Products: -
Products: -
r
4-bromocinnamyl alcohol + NADP+
4-bromocinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
4-chlorocinnamyl alcohol + NADP+
4-chlorocinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
4-coumaraldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-methoxybenzylalcohol + NADP+
4-methoxybenzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
4-methoxycinnamyl alcohol + NADP+
4-methoxycinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
4-methylcinnamyl alcohol + NADP+
4-methylcinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
5-hydroxyconiferyl aldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
Substrates: very low activity
Products: -
Products: -
?
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
5-hydroxyconiferyl aldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
5-hydroxyconiferylaldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
Substrates: very low activity
Products: -
Products: -
?
5-hydroxyconiferylaldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
Substrates: lowest catalytic efficiency
Products: -
Products: -
?
artemisinic aldehyde + NADPH + H+
artemisinic alcohol + NADP+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+
benzoic acid + NADPH
-
Substrates: the enzyme also shows dismutase activity
Products: -
Products: -
?
benzyl alcohol + NADP+
benzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
benzyl alcohol + NADP+
benzylaldehyde + NADPH + H+
Substrates: slight activity
Products: -
Products: -
r
benzylalcohol + NADP+
benzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
caffeoyl aldehyde + NADPH + H+
caffeoyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
caffeyl aldehyde + NADPH
caffeyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
caffeylaldehyde + NADP+
caffeyl alcohol + NADPH + H+
Substrates: low activity
Products: -
Products: -
?
caffeylaldehyde + NADPH + H+
caffeyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferol + NADP+
coniferyl aldehyde + NADPH
Substrates: -
Products: -
Products: -
?
coumaryl alcohol + NADP+
coumaraldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
p-coumarylaldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
Products: -
Products: -
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-coumaryl aldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: catalytic preference for 4-coumaraldehyde
Products: -
Products: -
?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
Substrates: high catalytic efficiency
Products: -
Products: -
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
Substrates: CAD4 displays slight activity for benzoyl alcohol
Products: -
Products: -
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
Substrates: -
Products: -
Products: -
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
Substrates: 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
Products: -
Products: -
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
Substrates: key enzyme in lignin biosynthesis
Products: -
Products: -
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
Substrates: involved in lignin biosynthesis
Products: -
Products: -
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: 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)
Products: 61% activity with 0.1 mM cinnamaldehyde, 7% activity with 1 mM cinnamaldehyde
Products: 61% activity with 0.1 mM cinnamaldehyde, 7% activity with 1 mM cinnamaldehyde
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
Substrates: the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
Products: -
Products: -
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: favourite substrate
Products: -
Products: -
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
Products: -
Products: -
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: 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
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: 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
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: 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
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH
coniferol + NADP+
-
Substrates: -
Products: -
Products: -
?
coniferyl aldehyde + NADPH
coniferol + NADP+
Substrates: -
Products: -
Products: -
?
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Substrates: CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
Products: -
Products: -
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
Substrates: recombinant enzyme encoded by gene GH2
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
Products: -
Products: -
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: the forward reaction is the physiological reaction
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: ?
Products: ?
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: best substrate
Products: -
Products: -
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: low activity
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: best substrate
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: ?
Products: ?
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: best substrate
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: ?
Products: ?
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Substrates: Bmr6 displays significantly greater activity in comparison to CAD4
Products: -
Products: -
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Substrates: 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
Products: -
Products: -
r
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaraldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapaldehyde + NADPH
-
Substrates: only CAD-C isoform
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: Bmr6 displays significantly greater activity in comparison to CAD4
Products: -
Products: -
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: 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
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: preferred substrate
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: recombinant enzyme encoded by gene GH2
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: ?
Products: ?
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: low activity
Products: -
Products: -
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: very low activity
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
sinapylaldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
sinapylaldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: role of the enzyme in lignin biosynthesis and structure formation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of isozyme CAD4
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of isozyme CAD4
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of isozyme CAD4
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of isozyme CAD5
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of isozyme CAD5
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of isozyme CAD5
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: substituted and unsubstituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme involved in lignification in vascular plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: methanol, ethanol, n-propanol, n-butanol, isobutanol, geraniol, various aromatic alcohols (e.g. salicyl alcohol, vanillyl alcohol, piperonyl alcohol)
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
Substrates: coniferylaldehyde and sinapylaldehyde are the preferred substrates
Products: -
Products: -
?
additional information
?
-
Substrates: coniferylaldehyde and sinapylaldehyde are the preferred substrates
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with methanol and ethanol as alcoholic substrates
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
Substrates: mo activity with sinapyl aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: mo activity with sinapyl aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: mo activity with sinapyl aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with sinapaldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with sinapaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with sinapaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: gene GH2 encodes a multifunctional enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: sinapaldehyde, 4-hydroxybenzaldehyde, vanillin, 4-hydroxy-3,5-dimethoxybenzaldehyde, 3,4-dimethoxybenzaldehyde, salicylaldehyde, 2-methoxybenzaldehyde, mannose, acetaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
Products: -
Products: -
?
additional information
?
-
Substrates: beta-glucuronidase expression driven by the CAD promoter is wound-inducible
Products: -
Products: -
?
additional information
?
-
-
Substrates: beta-glucuronidase expression driven by the CAD promoter is wound-inducible
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: liginification and lignin topochemistry indifferent samples, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
KJ159967
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
-
Substrates: PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
artemisinic aldehyde + NADPH + H+
artemisinic alcohol + NADP+
Substrates: -
Products: -
Products: -
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
Products: -
Products: -
?
coniferol + NADP+
coniferyl aldehyde + NADPH
Substrates: -
Products: -
Products: -
?
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
Products: -
Products: -
?
4-coumaric aldehyde + NADPH + H+
4-coumaric alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
Substrates: key enzyme in lignin biosynthesis
Products: -
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?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
Substrates: involved in lignin biosynthesis
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?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
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r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
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?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
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r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
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r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
Products: -
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?
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
Substrates: -
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r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
Substrates: -
Products: -
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r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
Substrates: the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
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?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
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?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
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?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
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?
cinnamyl aldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
Substrates: -
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?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
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r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
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r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Substrates: -
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r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Substrates: CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
Products: -
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
Products: -
Products: -
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Erianthus sp. IK 76-81
-
Substrates: -
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?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: the forward reaction is the physiological reaction
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: -
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Substrates: low activity
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
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r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: ?
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?
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
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r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
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r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
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r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
Substrates: -
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r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
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?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
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r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
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r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
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r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
Substrates: -
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r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: -
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Substrates: very low activity
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r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
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r
additional information
?
-
Substrates: role of the enzyme in lignin biosynthesis and structure formation
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?
additional information
?
-
Substrates: the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
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?
additional information
?
-
-
Substrates: the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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?
additional information
?
-
-
Substrates: enzyme involved in lignification in vascular plants
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
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?
additional information
?
-
Substrates: the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
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?
additional information
?
-
-
Substrates: the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
Products: -
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
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?
additional information
?
-
-
Substrates: final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
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?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
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?
additional information
?
-
-
Substrates: liginification and lignin topochemistry indifferent samples, overview
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
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?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
Products: -
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
cofactor binding site structure determination and analysis
NADP+
-
NADPH
-
dependent for, binding and specificity mechanism, interaction through Ser210, Arg211, and Lys215 and the terminal phosphate group
NADPH
cofactor binding site structure determination and analysis
NADPH
motif for both NADPH binding modelling
NADPH
-
NADPH
the NADPH binding sequence is located at amino acid residues 189-194
NADPH
the NADPH binding sequence is located at amino acid residues 188-193
NADPH
the NADPH binding sequence is located at amino acid residues 191-196
additional information
the enzyme has a highly conserved Rossmann fold NAD(P)H/NAD(P)+ binding domain
-
additional information
-
the enzyme has a highly conserved Rossmann fold NAD(P)H/NAD(P)+ binding domain
-
additional information
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
additional information
-
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
additional information
-
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
additional information
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
-
activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+
EDTA
-
activates at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
additional information
Zn2+
zinc-type enzyme, ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
required, the enzyme contains the Zn-1 binding domain motif GHE(X)2G(X)5G(X)2V and the conserved Zn-1 catalytic residues C47, H69, and C163
Zn2+
required, Zn1 binding sequence is located at amino acid residues 69-83, and Zn2 binding sequence is located at amino acid residues 89-114
Zn2+
required, Zn1 binding sequence is located at amino acid residues 68-82, and Zn2 binding sequence is located at amino acid residues 88-113
Zn2+
required, Zn1 binding sequence is located at amino acid residues 71-85, and Zn2 binding sequence is located at amino acid residues 91-116
Zn2+
required, Zn1 binding sequence is GHE(X)2G(X)5G(X)2V located at amino acid residues 68-82, and Zn2 binding sequence GD(X)9,10C(X)2C(X)2(X)7C located at amino acid residues 88-114, structural zinc coordinated residue are Cys100, Cys103, Cys106, and Cys114
Zn2+
4 Zn2+ per homodimer, the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions
Zn2+
required, motif for both Zn2+ binding, modelling
Zn2+
required
Zn2+
-
restores activity after incubation in buffer containing a divalent-cation exchange resin
Zn2+
-
required, Zn1-binding motif [GHE(X)2G(X)5G(X)2 V] and Zn2-binding motif [GD(X)9,10C(X)2C(X)2C(X)7C] occur in most of the isozymes, overview
Zn2+
require, the TaCAD12 protein contains one alcohol dehydrogenase domain (42-157 aa) with two Zn binding sites (41-63 and 76-90 aa) and one Zn-binding dehydrogenase domain (199-323 aa)
additional information
slight activating effect by KCl at 100 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-monophosphate
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
cinnamaldehyde
-
substrate inhibition mediated by cinnamaldehyde concentrations far from the Km value of 0.46 mM, which does not allow for excessively increasing the starting cinnamaldehyde concentration, since the process yield may be greatly affected
Ni
-
CAD activity is not affected by concentrations up to 0.12 mM, phenolic metabolism is not substantially affected by Ni excess
RNAi
-
RNAi-mediated transient gene silencing in the epidermis leads to a higher penetration efficiency of Blumeria graminis f. sp. tritici (64%) than in the controls. Gene silencing also compromises penetration resistance to varying degrees with different genes against an inappropriate pathogen, Blumeria graminis f. sp. hordei. Co-silencing of CAD and other genes involved in monolignol biosynthesis leads to greater penetration of Blumeria graminis f. sp. tritici or Blumeria graminis f. sp. hordei than when the genes are silenced separately. Gene silencing hamperes host autofluorescence response at fungal contact sites
-
coniferyl aldehyde
competitve, a stronger inhibitor than sinapyl aldehyde; competitve, a stronger inhibitor than sinapyl aldehyde; competitve, a stronger inhibitor than sinapyl aldehyde
sinapyl aldehyde
competitve, a weaker inhibitor than coniferyl aldehyde; competitve, a weaker inhibitor than coniferyl aldehyde; competitve, a weaker inhibitor than coniferyl aldehyde
Zn2+
-
inhibitory at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions, strong inhibition
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves results in reduced penetration resistance against Puccinia hordei infection
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves has no efffect in on resistance against Puccinia hordei infection
additional information
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
additional information
-
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO2
-
high CO2 stimulates progressively the enzyme, as well as of other enzymes involved in metabolism of phenolic compounds, overview
jasmonate
accumulation of CAD mRNA in response to jasmonate application and mechanical wounding
additional information
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
-
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
-
Cinnamyl alcohol dehydrogenase activity remains unaffected by both methyl jasmonate and salicylic acid. This indicates that methyl jasmonate and salicylic acid induce the accumulation of phenolic compounds in ginseng root by altering the phenolic synthesis enzymes
-
additional information
-
the enzyme is not nduced by stress, but is related to cell wall lignification
-
additional information
-
mechanical stress application induces a strong increase of CAD activity in rubbed internode with an approximately 2fold increase when compared to control tomato internodes. Increased activity of CAD is associated with a higher lignin content in the rubbed internode
-
additional information
-
CAD transcripts are accumulated in response to infection with Blumeria graminis f. sp. tritici. Accumulates at 6 hpi, followed by a slight decrease at 12 hpi and then a sharp increase at 24 hpi
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
cinnamyl-alcohol dehydrogenase deficiency
Identification of the structure and origin of thioacidolysis marker compounds for cinnamyl alcohol dehydrogenase deficiency in angiosperms.
cinnamyl-alcohol dehydrogenase deficiency
Signatures of cinnamyl alcohol dehydrogenase deficiency in poplar lignins.
Dwarfism
Identification of Transcription Factors Involved in Rice Secondary Cell Wall Formation.
Infections
A Wheat Cinnamyl Alcohol Dehydrogenase TaCAD12 Contributes to Host Resistance to the Sharp Eyespot Disease.
Mycoses
Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes during development and following fungal infection in Populus.
Prostatic Neoplasms
Angiomotin is a novel component of cadherin-11/?-catenin/p120 complex and is critical for cadherin-11-mediated cell migration.
Prostatic Neoplasms
Cadherin-11 endocytosis through binding to clathrin promotes cadherin-11-mediated migration in prostate cancer cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0244
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0891
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0042
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.013
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
0.036
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.114
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
0.117
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
0.00266
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
0.06975
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
31
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
1
benzyl alcohol
-
isoform CAD1, pH and temperature not specified in the publication
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
0.01425
cinnamaldehyde
pH 6.0, 30°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
0.03115
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.08554
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.00098
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0075
coniferyl alcohol
pH 8.8, temperature not specified in the publication
0.117
coniferyl alcohol
pH 8.8, temperature not specified in the publication
0.0038
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.00437
coniferyl aldehyde
isoform CAD2, at pH 6.3 and 30°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
0.0085
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
0.0109
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
0.028
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
0.032
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
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
0.008
p-coumaryl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0094
p-coumaryl aldehyde
-
wild-type Mt-CAD2, pH and temperature not specified in the publication
0.0272
p-coumaryl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.06095
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.09157
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.0156
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0043
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
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
0.0078
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
0.026
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
0.0406
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
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
KJ159967
steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.7
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.026
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
6.8
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
40.2
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
74.2
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.069
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
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
2.5
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
0.062
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.072
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.188
cinnamyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
0.311
cinnamyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
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
13.2
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.00098
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0121
coniferyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.032
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.1
coniferyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
0.154
coniferyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
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
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
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
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
0.46
p-coumaryl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
15.6
p-coumaryl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.005
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.006
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
46.4
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.00135
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0053
sinapyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.024
sinapyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
0.039
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
0.041
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.044
sinapyl aldehyde
-
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
0.073
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
3.63
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.169
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.082
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
5880
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.23
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
345
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
523
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
2061
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.28
4-coumaryl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
0.38
4-coumaryl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
0.46
4-coumaryl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
0.47
4-coumaryl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
0.51
4-coumaryl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
0.52
4-coumaryl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
7.5
4-coumaryl aldehyde
isoform CAD6, at pH 6.3 and 30°C
26.3
4-coumaryl aldehyde
isoform CAD7, at pH 6.3 and 30°C
40
4-coumaryl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
170
4-coumaryl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
370
4-coumaryl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
1540.5
4-coumaryl aldehyde
isoform CAD2, at pH 6.3 and 30°C
3.273
4-coumarylaldehyde
isoform CAD1, at pH 6.0 and 25°C
7.136
4-coumarylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.0448
5-hydroxyconiferylaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.054
5-hydroxyconiferylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.766
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.935
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
11.5
cinnamyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
13.7
cinnamyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
2369
cinnamyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
0.993
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
2.322
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
13400
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0306
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.4
coniferyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
0.896
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
1.32
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
9.7
coniferyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
10
coniferyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
10
coniferyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
10.62
coniferyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
15.3
coniferyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
25.3
coniferyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
40
coniferyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
59.4
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
90
coniferyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
130
coniferyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
140
coniferyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
220
coniferyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
390
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
920
coniferyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
1070
coniferyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
2202
coniferyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
7154.8
coniferyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
10200
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
35800
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
268200
coniferyl aldehyde
pH 6.0, 30°C, recombinant enzyme
0.25
p-coumaryl aldehyde
pH not specified in the publication, temperature not specified in the publication
48.9
p-coumaryl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
1950
p-coumaryl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.063
sinapaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.075
sinapaldehyde
isoform CAD2, at pH 6.0 and 25°C
2980
sinapyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0245
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0328
sinapyl aldehyde
-
Mt-CAD2, pH and temperature not specified in the publication
0.14
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
0.156
sinapyl aldehyde
-
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
0.286
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.354
sinapyl aldehyde
-
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
0.45
sinapyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
1.58
sinapyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
1.8
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
5.39
sinapyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
6.8
sinapyl aldehyde
isoform CAD6, at pH 6.3 and 30°C
10
sinapyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
21.2
sinapyl aldehyde
isoform CAD7, at pH 6.3 and 30°C
40
sinapyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
180
sinapyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
200
sinapyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
310
sinapyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
360
sinapyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
380
sinapyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
530
sinapyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
926
sinapyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
1025
sinapyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
3858
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
3859
sinapyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme
5352.3
sinapyl aldehyde
isoform CAD2, at pH 6.3 and 30°C
13600
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
20500
sinapyl aldehyde
pH not specified in the publication, temperature not specified in the publication
198900
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.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.099
4-coumaryl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
0.16
4-coumaryl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
7.63
4-coumaryl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
10.02
4-coumaryl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
20.59
4-coumaryl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
31.92
4-coumaryl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
32.67
4-coumaryl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.0121
coniferyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
0.0162
coniferyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
0.123
coniferyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.295
coniferyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
0.295
coniferyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
0.427
coniferyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
0.711
coniferyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
4.17
coniferyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
6.03
coniferyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
0.0374
sinapyl aldehyde
isoform CAD4 mutant Y95V, at pH 6.5 and 30°C
0.083
sinapyl aldehyde
wild type isoform CAD2, at pH 6.5 and 30°C
0.118
sinapyl aldehyde
wild type isoform CAD4, at pH 6.5 and 30°C
1.056
sinapyl aldehyde
isoform CAD4 mutant L119W, at pH 6.5 and 30°C
1.23
sinapyl aldehyde
isoform CAD4 mutant G301F, at pH 6.5 and 30°C
1.39
sinapyl aldehyde
isoform CAD4 mutant Y288P, at pH 6.5 and 30°C
1.455
sinapyl aldehyde
isoform CAD4 mutant W58L, at pH 6.5 and 30°C
2.91
sinapyl aldehyde
isoform CAD4 mutant A278V, at pH 6.5 and 30°C
68.08
sinapyl aldehyde
isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.58
adenosine 5'-monophosphate
Eucalyptus gunnii
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity in roots at different CO2 concentrations for different periods of time, overview
additional information
-
relative enzyme activity in different sharp eyespot-resistant and -susceptive lines/cultivars
additional information
relative enzyme activity in different sharp eyespot-resistant and -susceptive lines/cultivars
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
aldehyde reduction
5.5
6.25
6.5
7.5
7.6
8.8
6
aldehyde reduction
6
-
optimum for cinnamaldehyde reduction, whereas oxidation of ethanol and 2-propanol is best accomplished at pH 9, pH 7 is a satisfactory compromise
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 9
profile overview
4 - 8.5
profile overview
4.5 - 7.5
activity range, profile overview
4.5 - 8.5
-
pH 4.5: about 55% of activity maximum, pH 8.5: about 30% of activity maximum
5.5 - 8.5
activity range, the enzyme is completely inactive at pH 5.0 and pH 9.0, profile overview
6 - 8
-
coniferyl aldehyde reduction, pH 6.0: about 70% of activity maximum, pH 8.0: about 30% of activity maximum
7.2 - 9.7
-
coniferyl alcohol oxidation, pH 7.2: about 40% of activity maximum, pH 9.7: about 35% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
aldehyde reduction
25
30
37
40
50
aldehyde reduction
30
aldehyde reduction
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
very high activity at 10-40°C, rapid decrease in activity above 40°C, profile overview
10 - 50
activity range, profile overview
10 - 55
very high activity at 30-50°C, profile overview
30 - 42
-
good activity between 30°C to 42°C with maximum activity at 40°C, beyond which activity declined sharply
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.76
sequence calculation
5.9
6.15
sequence calculation
6.24
sequence calculation
6.28
sequence calculation
6.43
sequence calculation
6.48
sequence calculation
6.5
6.67
sequence calculation
7.97
sequence calculation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Fxcad1; cv. Chandler, octaploid cultivar, gene Fxcad1 and Fxcad2
SwissProt
brenda
neoformed calli induced by Agrobacterium rhizogenes on Phaseolus mungo hypocotyl
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expression pattern of isoforms Cad-4, Cad-5 is consistent with development/formation of different forms of the lignified vascular apparatus and expression is also indicative of a role in plant defense. Expression of isoforms Cad-7, Cad-8 resembles largely those of isoforms Cad-4, Cad-3 indicating a minor role in lignin formation. Isoforms Cad-1 and Cad-9 lack detectable catalytic activities and are expressed predominantly in vascular tissue
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cv. K-29, from the garden of Department of Biochemistry, Lucknow University, India
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with a high-molecular-mass elicitor preparation heat-released from mycelial cell walls
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yellow-fleshed NMF Oro A and MF Springcrest, and blood-flesh MF Sanguinella
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induced with elicitor from Puccinia graminis f. sp. tritici germ tube walls
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isoform TaCAD1 belonging to the bona fide CAD group involved in lignin synthesis
UniProt
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sharp eyespot-resistant and -susceptive lines/cultivars
UniProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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shell zone, immunogold-electron microscopy of shoot apex
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CAD is accumulated in the epidermis, CAD gene expression after pathogen attack is predominantly in the epidermis
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immunogold-electron microscopy of shoot apex
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developing, immunogold-electron microscopy of shoot apex
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immunogold-electron microscopy of mature stems
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immunogold-electron microscopy of shoot apex
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predominant expression of isoforms Cad-1, Cad-9
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additional information
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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
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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
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all CAD genes expressed, but at different levels. Very low expression of CAD7
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highest expression level in buds
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very high expression level in buds
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immunogold-electron microscopy of mature stems
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highest CAD1 expression level in mature flowers
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high levels of CAD activity/expression in Sanguinella, a blood flesh cultivar, phenolics and lignin contents and CAD activities, overview
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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
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Bmr6 expression in young internodes is significantly higher than CAD4 for all genotypes
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highest expression of isoforms CAD3, CAD5, CAD6 and CAD8
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FC1 is expressed slightly more at the seedling stage than at the heading stage
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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
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isoforms Cad-4, Cad-5, expression in root caps. Isoforms Cad-2, Cad-3, expression in non-lignifying root tips
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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
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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
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FC1 is expressed slightly more at the seedling stage than at the heading stage
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greatest expression in the root
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quantitative realtime PCR enzyme expression analysis during seed development, overview. CAD2 shows the highest expression level of all three CAD isozymes in Carthamus tinctorius
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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
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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
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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
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mRNA is more abundant in the lower stem than in the upper stem
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transcriptional patterns of TaCAD12 in wheat stems after Rhizoctonia cerealis inoculation analyzed by quantitative RT-PCR, overview
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LtuCAD1 has the highest expression level in xylem
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the native CAD gene is preferentially expressed in differentiating xylem both in stems and roots
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young, immunogold-electron microscopy of mature stems
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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
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additional information
enzyme expression pattern of AtCAD-C and AtCAD-D, no expression in silique
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additional information
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quantitative RT-PCR expression analysis, in the Bd4179 mutant, only internodes and peduncles show detectable activity
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additional information
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differential expression of CmCADs, CmCAD2 is strongly expressed in flesh during development
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additional information
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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
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additional information
tissue expression study, no enzyme expression in root
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additional information
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tissue expression study, no enzyme expression in root
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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
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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
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additional information
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promoter expression is barely detecable in cotyledons. Weak expression is observed in lignified tissues of vascular system of mature leaves and stems
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additional information
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promoter expression is barely detecable in cotyledons. Weak expression is observed in lignified tissues of vascular system of mature leaves and stems
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additional information
quantitative RT-PCR enzyme expression analysis. LtuCAD1 is differentially expressed in vascular tissues
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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
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
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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
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
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additional information
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expression analysis of CAD/CAD-like genes, overview. PtoCAD1 is the most abundantly expressed in each tissue
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
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additional information
no obvious expression variation in the expression of PtoCAD2
brenda
additional information
KJ159967
no obvious expression variation in the expression of PtoCAD2
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additional information
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no obvious expression variation in the expression of PtoCAD2
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
brenda
additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview
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additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview
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additional information
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expression analysis of CAD/CAD-like genes, overview
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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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
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additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
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expression analysis of CAD/CAD-like genes, overview. PtoCAD5 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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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
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additional information
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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additional information
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expression analysis of CAD/CAD-like genes, overview. PtoCAD7 is expressed at low levels in all tissues
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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
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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
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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
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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
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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
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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
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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
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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
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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
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additional information
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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
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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
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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
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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
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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
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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
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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
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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
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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
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additional information
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expression analysis of CAD/CAD-like genes, overview. Moderate expression in all tissues of PtoCAD9, except for the very high expression in buds
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additional information
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
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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
KJ159967
expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
brenda
additional information
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expression analysis of CAD/CAD-like genes, overview. PtoCAD12 is moderately expressed in all tissues with no obvious preference
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additional information
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CAD2, CAD3, CAD5, CAD6, CAD11, CAD14, CAD15 show no significant expression differences between tissues
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additional information
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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
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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
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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
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additional information
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transcriptional levels of TaCAD12 in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
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additional information
transcriptional levels of TaCAD12 in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
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additional information
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neoformed calli induced by Agrobacterium rhizogenes on Phaseolus hypocotyl
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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14 of the 15 CAD genes are distributed on duplicated regions
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no typical signal peptides are found in all CmCADs, CmCAD proteins may locate in the cytoplasm
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the enzyme contains no N-terminal targeting sequence
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Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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a total of 24 putative full-length PRUPE_CAD genes are identified (in silico analysis) in the peach genome, overview
evolution
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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
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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
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties
evolution
flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
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
TaCAD12 belongs to IV group in 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
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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
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purified CAD by MALDI-TOF shows a significant homology to alcohol dehydrogenases of MDR superfamily
evolution
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flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
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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
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
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
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
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
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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
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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
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
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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
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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
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metabolism
cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase catalyze key steps in the pathway of lignin monomer biosynthesis
metabolism
enzyme CAD catalyzes the final step in monolignol biosynthesis, leading to lignin formation in plants
metabolism
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cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
cinnamyl alcohol dehydrogenase is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
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
cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis and catalyzes the final step in the synthesis of monolignols
metabolism
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cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis
metabolism
the enzyme is responsible for lignin biosynthesis
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
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cinnamyl alcohol dehydrogenase is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
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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
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
-
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
hydroxycinnamaldehyde content is a more important determinant of digestibility than lignin content
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
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
enzyme CAD plays a role in defense responses to necrotrophic or soil-borne pathogens in wheat
physiological function
-
involvement of BdCAD1 in lignification. Wild-type BdCAD1 rescues the altered lignin profile of Arabidopsis and Brachypodium CAD mutants
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
-
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. 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. 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. 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
-
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
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
isoform CAD6 is involved in developmental lignification in rice and also plays a role in the defense response against rice pathogens
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
-
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
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
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
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
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
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
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
lignin and sugar content and composition during stem development, overview
additional information
lignin and sugar content and composition during stem development, 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 molecular docking analysis with substrates, active site structure, structure comparisons between isozymes, overview
Show AA Sequence and Transmembrane Helices (1942 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33460
-
34000
38624
x * 38624, calculated. x * 42500, SDS-PAGE of His-tagged protein
38700
39000
39050
-
39350
-
40000
42500
x * 38624, calculated. x * 42500, SDS-PAGE of His-tagged protein
44000
80000
34000
-
40000
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
x * 39600, isoform CAD7, calculated from amino acid sequence
?
x * 38600, isoform CAD2, calculated from amino acid sequence
?
x * 39100, isoform CAD6, calculated from amino acid sequence
?
x * 40000, about, SDS-PAGE, x * 389400, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 389700, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 39270, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 39050, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 39350, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 39290, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 38540, sequence calculation
?
x * 40000, about, SDS-PAGE, x * 339420, sequence calculation
?
x * 34000, about, SDS-PAGE, x * 33460, sequence calculation
homodimer
2 * 35700, isoform CAD1, calculated from amino acid sequence
homodimer
2 * 36900, isoform CAD2, calculated from amino acid sequence
additional information
structure analysis of isozyme CAD4 by dynamic light scattering
additional information
structure analysis of isozyme CAD4 by dynamic light scattering
additional information
-
structure analysis of isozyme CAD4 by dynamic light scattering
additional information
structure analysis of isozyme CAD5 by dynamic light scattering
additional information
structure analysis of isozyme CAD5 by dynamic light scattering
additional information
-
structure analysis of isozyme CAD5 by dynamic light scattering
additional information
-
enzyme interacts with glycine-rich protein AtGRP9 that is expressed in vascular tissue of the root and localized to cell wall and cytoplasm
additional information
the dimer shows 12 free and 16 totalcysteine residues. Two disulfide linkages can be deduced per dimer from the data, one intra-subunit linkage per subunit, and one non-interchain linkage
additional information
-
the dimer shows 12 free and 16 totalcysteine residues. Two disulfide linkages can be deduced per dimer from the data, one intra-subunit linkage per subunit, and one non-interchain linkage
additional information
-
alpha-helical and beta-strand segments of Mt-CAD2, modelling, overview
additional information
-
analysis of the apo and holo enzyme structures
additional information
-
the TaCAD12 protein contains one alcohol dehydrogenase domain (42-157 aa) with two Zn binding sites (41-63 and 76-90 aa) and one Zn-binding dehydrogenase domain (199-323 aa) with one highly conserved motif (196GLGGLG201) in CAD. The motif GLGGLG participates in binding the diophosphate group of NADP+
additional information
the TaCAD12 protein contains one alcohol dehydrogenase domain (42-157 aa) with two Zn binding sites (41-63 and 76-90 aa) and one Zn-binding dehydrogenase domain (199-323 aa) with one highly conserved motif (196GLGGLG201) in CAD. The motif GLGGLG participates in binding the diophosphate group of NADP+
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant isozyme CAD5, 4-10 mg/ml apo-protein in 20 mM Tris-HCl, pH 8.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, at 4°C or at 20°C, 2fold dilution with reservoir solution containing 20% w/v PEG 3350, and 0.2 M trilithium citrate tetrahydrate, pH 8.1 3 days, X-ray diffraction structure determination an analysis at 2.0-2.6 A resolution
in complex with NADP(H), to 2.18 A resolution. NADP(H) is bound through hydrophobic interactions within the well-conserved GXGGXG motif from residues Gly184 to Gly189 and the adenine ring is the syn-conformation and is sandwiched between the guanidino group of Arg208 and Thr244 side chains. The aromatic side chains of residues Phe114 and Tyr116 in the active site could bind aromatic aldehydes by stacking the aromatic head of the substrates
D0ITF8
homology modeling based on structure of Arabidopsis thaliana isoform CAD5. The model reveals a trilobed structure. The two major lobes contribute to constitution of NADP+ binding, catalytic Zn2+ binding and substrate binding domains. The substrate binding pocket is protected by these two major lobes and is in close proximity of catalytic Zn2+ and NADP+ binding domains
10 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml of both protein and reservoir solution, the latter containing 1. 1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, or 2.30% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, room temperature, about 1 week, trigonal or monoclinic crystals, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
isoform CAD4, hanging drop vapor diffusion method, using 2% (v/v) tacsimate, pH 7.0, 5% (v/v) 2-propanol, 0.1 M imidazole, pH 7.0, and 8% (w/v) polyethylene glycol 3350
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
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, 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
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
-
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
-
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
-
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
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
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
-
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-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%
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%
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
-
up to 30°C, retains all initial catalytic activity, only 18% activity is lost at 40°C, at 60°C 100% loss of activity
40
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
60% loss of activity after 20 h incubation in buffer containing a divalent cation-exchange resin
-
freezing of glycerol containing fractions causes 50% loss of activity after 24 h
-
the enzyme is resistant to osmolytes, reducing agents and non-ionic detergents
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant His-tagged enzyme, 75 mM sodium phosphate, pH 7.5, 5 mM DTT, no loss of activity after 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 514.2fold from secondary xylem by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and affinity chromatography (elution with NADP+)
-
Ni-NTA agarose column chromatography and Mono Q column chromatography
Ni-NTA column chromatography
recombinant enzyme from strain BL9 by DEAE ion exchange, Red-Sepharose, and gel filtration chromatography
-
recombinant GST-fusion enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography
recombinant His-tagged enzyme 65fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, anion exchange chromatography, and again gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chrmatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged PtoCAD1 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged PtoCAD2 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged PtoCAD3 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged PtoCAD5 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged PtoCAD7 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged PtoCAD9 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged wild-type and mutant Mt-CAD2 enzymes by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration
-
recombinant His-tagged wild-type Mt-CAD1 enzyme by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.3 kb cDNA fragment cloned into pGEM-T Easy vector and transformed into competent cell of DH5alpha from Escherichia coli
9 AtCAD genes, 2 paralogs AtCAD-C and AtCAD-D, DNA and amino acid sequence determination and analysis, tissue expression pattern study of wild-type and mutant plants
construct pCFC1 containing the entire 8.8 kb open reading frame, 3253 bp upstream sequences, and the 1646 bp downstream region and an empty pCAMBIA2301 vector introduced into the fc1 mutant by Agrobacterium tumefaciens-mediated transformation
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 Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) 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, isozyme genotyping, phylogenetic analysis, sequence comparisons, and expression analysis of isozymes
-
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
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
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
drought stress causes 25% decrease in the transcript level of isoforms CAD3 in leaves, CAD4 in stems and CAD8 in roots. A reduced level of transcript is observed for isoforms CAD7 and CAD8 under cold stress (10°C). 25% or more reduction in the transcript level is observed after inoculation with Fusarium oxysporum sp. linii for isoform CAD6 and 8 in leaves, CAD4 in stems (66% decrease) and CAD6 (43% decrease) in roots. In stems and roots of plants 4 days after inoculation the silencing of isoform CAD expression is stronger, around 40% or more for: CAD1A and B, CAD4 and CAD5 in stems, CAD1A, LuCAD8, LuCAD4, LuCAD6 and LuCAD7
drought stress causes general increase in the transcript level of nearly all enzyme isoforms in all tissues in comparison to the control. The highest increase in the expression, around 2fold that of the control, is observed for isoforms CAD1A, CAD2, CAD5, CAD6 and CAD8 both in leaves and stems. In leaves, the increase in the mRNA level is observed for all enzyme isoforms under cold stress (10°C). The highest transcript accumulation was observed for CAD1B (5fold), CAD1A (4fold) and CAD2 (2fold). In stems, cold induces the expression of CAD1B and CAD1A (2fold) In roots, an increase in the expression of enzyme is observed for CAD5 (5times the control level) and CAD1B (3fold). UV radiation treatment causes increased expression of all analyzed isoforms in leaves, 21-69% more than in the control. Four days after inoculation with Fusarium oxysporum sp. linii, isoform CAD1A shows the highest increase of expression (over 30% more than the control). Also, the induction isoform CAD expression is observed in roots 24 h after inoculation (CAD1B and CAD5) and in stems 96 h after inoculation, where the mRNA level of isoform CAD2 increases 3fold, CAD6 6fold and CAD7 5fold
expression of isoform CAD3 is strongly up-regulated in tea plants after Ectropic oblique attack and mechanical damage. Presence of abscisic acid induces isoform CAD3 expression
gene transcripts are highly induced by cold, wounding, and reactive oxygen species. Promoter activity is strongly induced in response to the biotic and abiotic stresses, with the strongest inducer being wounding, and is also induced by salicylic acid and jasmonic acid as well as by abscisic acid and 6-benzylaminopurine
H2O2 and drought stress, and slightly also abscisic acid induce CAD1 expression
inoculation of sugarcane stems with Sporisorium scitamineum elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
methyl jasmonate and salicylic acid elevate the expression of isoform CAD1
methyl jasmonate and salicylic acid elevate the expression of isoform CAD2
methyljasmonate, and drought stress suppress CAD1 expression
mRNA is highly expressed in stems at the elongation and heading stages. At the milky stage of wheat, CAD1 mRNA abundance, protein level and enzyme activity in stem tissues are higher in lodging-resistant cultivar H4546 than in lodging-sensitive cultivar C6001
presence of abscisic acid does not induce isoform CAD2 expression
presence of Zn2+ is essential for the expression of enzyme, as no expression is observed in absence of Zn2+
the CAD genes are strongly upregulated by methyljasmonate, transcriptome analysis, overview
-
the CAD genes are strongly upregulated by methyljasmonate, transcriptome analysis, overview. Accumulation of ptox and lignin in PhCAD1-4 isoforms overexpressing transgenic lines, overview
-
the enzyme expression is upregulated in roots, stems and leaves during cadmium treatment (0.03 mM)
-
the enzyme is induced by infection with Rhizoctonia cerealis, a necrotrophic fungus that causes the sharp eyespot disease in wheat. Transcriptional levels of TaCAD12 in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
the expression of isoform CAD2 is induced by biotic and abiotic stresses such as Xanthomonas oryzaepv. oryzae infection and UV-irradiation
the expression of isoform CAD6 is induced by biotic and abiotic stresses such as Xanthomonas oryzaepv. oryzae infection and UV-irradiation
the expression of isoforms CAD1 and CAD2 is induced by methyl jasmonic acid treatment
the expression of PaCAD1 is induced by methyl jasmonic acid (MeJA) treatment by about 2fold
the expression of PaCAD2 is induced by methyl jasmonic acid (MeJA) treatment by up to 7fold
the expression of the enzyme gene is upregulated in silicon- and paclobutrazol-treated plants
the transcriptional levels of the enzyme in sharp eyespot-resistant wheat lines are significantly higher compared with those in susceptible wheat lines
treatment of seedling with exogenous abscisic acid, salicylic acid, ethephon, ultraviolet and wounding leads to increase in expression
wounding, cold, H2O2, salt, and drought stresses, salicylic acid, and abscisic acid induce CAD1 expression
wounding, methyljasmonate, and cold stress suppress CAD1 expression
gene transcripts are highly induced by cold, wounding, and reactive oxygen species. Promoter activity is strongly induced in response to the biotic and abiotic stresses, with the strongest inducer being wounding, and is also induced by salicylic acid and jasmonic acid as well as by abscisic acid and 6-benzylaminopurine
-
gene transcripts are highly induced by cold, wounding, and reactive oxygen species. Promoter activity is strongly induced in response to the biotic and abiotic stresses, with the strongest inducer being wounding, and is also induced by salicylic acid and jasmonic acid as well as by abscisic acid and 6-benzylaminopurine
-
-
inoculation of sugarcane stems with Sporisorium scitamineum elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
-
inoculation of sugarcane stems with Sporisorium scitamineum elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
-
-
inoculation of sugarcane stems with Sporisorium scitamineum elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biofuel production
downregulation of (hydroxy)cinnamyl alcohol dehydrogenase (CAD) genes is another promising strategy to increase cell wall digestibility for biofuel production
biotechnology
the spruce CAD promoter represents a valuable tool for research and biotechnology applications related to xylem and wood
industry
-
cofactor recycling catalytic system reveals both 100% selectivity and aldehyde conversion within 3 h by usage of ADH, which provides an inexpensive overall process
nutrition
-
Increased bamboo shoot firmness during cold storage is positively correlated with higher lignin and cellulose accumulation, and this accumulation of lignin in flesh tissue is also positively correlated with the activities of phenylalanine ammonia lyase, cinnamyl alcohol dehydrogenase and peroxidase. Ethylene treatment is associated with higher disease incidence, chilling injury index, electrical conductivity, respiration and ethylene production, enhanced lignin and cellulose accumulation and accelerates the activities of phenylalanine ammonia lyase, cinnamyl alcohol dehydrogenase and peroxidase. In contrast, 1-methylcyclopropene treatment is associated with lower respiration, ethylene production, chilling injury index and electrical conductivity, reduced lignin and cellulose accumulation and retards the activities of phenylalanine ammonia lyase, cinnamyl alcohol dehydrogenase and peroxidase. 1-Methylcyclopropene may be used commercially to control disorders in bamboo shoot during cold storage
synthesis
additional information
agriculture
-
gene GH2 can be useful in engineering of rice, to optimize the important crop plant
agriculture
-
treament of leaves with cinnamyl alcohol dehydrogenase inhibitor [[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester results in reduced penetration resistance against Puccinia hordei infection
agriculture
-
treament of leaves with cinnamyl alcohol dehydrogenase inhibitor [[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester has no effect on resistance against Puccinia hordei infection
agriculture
-
putative single nucleotide polymorphisms can be developed as single nucleotide polymorphisms markers for quantitative trait loci detection in Acacia hybrid mapping populations after validation using segregation analysis. Selecting favourable alleles from progenies which produce desirable lignin profiles will be advantageous in tree breeding programmes for plantation establishment
agriculture
-
putative single nucleotide polymorphisms can be developed as single nucleotide polymorphisms markers for quantitative trait loci detection in Acacia hybrid mapping populations after validation using segregation analysis. Selecting favourable alleles from progenies which produce desirable lignin profiles will be advantageous in tree breeding programmes for plantation establishment
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation
agriculture
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%
agriculture
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%
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation. The resistance of My5514 to Sporisorium scitamineum is likely derived, at least in part, to a marked increase of lignin concentration by the activation of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation
-
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation. The resistance of My5514 to Sporisorium scitamineum is likely derived, at least in part, to a marked increase of lignin concentration by the activation of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
-
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation
-
agriculture
-
cultivar My5514 is resistant to Sporisorium scitamineum, whereas B42231 is susceptible to the pathogen. Inoculation of sugarcane stems elicits lignification and produces significant increases of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase. Production of lignin increases about 29% in the resistant cultivar and only 13% in the susceptible cultivar after inoculation. The resistance of My5514 to Sporisorium scitamineum is likely derived, at least in part, to a marked increase of lignin concentration by the activation of coniferyl alcohol dehydrogenase and sinapyl alcohol dehydrogenase
-
synthesis
-
synthesis of cinnamyl alcohol from cinnamaldehyde using the isolated enzyme or by expression of enzyme in Escherichia coli. The reduction of cinnamaldehyde by the isolated enzyme occurrs in 3 h at 50°C with 97% conversion, and yields high purity cinnamyl alcohol with a yield of 88% and a productivity of 50 g/g enzyme. The reduction of 12.5 g/l cinnamaldehyde by whole cells in 6 h, at 37 °C and no requirement of external cofactor occurrs with 97% conversion, 82% yield of 98% pure alcohol and a productivity of 34 mg/g wet cell weight
synthesis
-
potential exploitation of rationally engineered forms of CAD2 for the targeted modification of monolignol composition in transgenic plants
additional information
CAD is a useful tool to improve lignin digestibility and/or to lower the lignin levels in plants. Enzyme knockout modification targeted directly to block lignin synthesis causes not only reduced lignin level in fibre, but also affects amount and organization of cellulose and pectin. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality. Such plants can be successfully cultivated in a field
additional information
-
CAD is a useful tool to improve lignin digestibility and/or to lower the lignin levels in plants. Enzyme knockout modification targeted directly to block lignin synthesis causes not only reduced lignin level in fibre, but also affects amount and organization of cellulose and pectin. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality. Such plants can be successfully cultivated in a field
additional information
-
CAD is a useful tool to improve lignin digestibility and/or to lower the lignin levels in plants. Enzyme knockout modification targeted directly to block lignin synthesis causes not only reduced lignin level in fibre, but also affects amount and organization of cellulose and pectin. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality. Such plants can be successfully cultivated in a field
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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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 (U3TI46), Carthamus tinctorius (U3TH11), Carthamus tinctorius (U3TDQ6)
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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 (T1WW82), Populus tomentosa (T1WUU2), Populus tomentosa (T1WVG5), Populus tomentosa (T1WWB9), Populus tomentosa (T1WWR8), Populus tomentosa (A0A023RBJ1), Populus tomentosa (T1WW77), Populus tomentosa (T1WUT6), Populus tomentosa (KJ159967), 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
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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
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