1.1.1.195: cinnamyl-alcohol dehydrogenase
This is an abbreviated version!
For detailed information about cinnamyl-alcohol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.195
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1.1.1.195
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lignin
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lignification
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monolignols
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phenylpropanoids
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sinapyl
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xylem
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coniferyl
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ammonia-lyase
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cinnamoyl-coa
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caffeic
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coniferaldehyde
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guaiacyl
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sinapaldehyde
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eucalyptus
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cinnamoyl
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hydroxycinnamyl
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linum
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taeda
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p-coumaryl
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cinnamaldehydes
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syringyl
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loblolly
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biofuel production
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nutrition
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industry
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biotechnology
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4-coumarate-coa
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4.3.1.5
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synthesis
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thioacidolysis
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4-coumarate
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3-o-methyltransferase
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podophyllotoxin
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agriculture
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gunnii
- 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
Reaction
Synonyms
ADH, AdhA, alcohol dehydrogenase, AtCAD4, BdCAD1, Bmr6, Bradi3g06480, brown midrib6, Brown-midrib 1 protein, CAD, CAD 7/8, CAD1, CAD10, CAD11, CAD12, CAD13, CAD14, CAD15, CAD2, CAD3, CAD4, CAD5, CAD6, CAD7, CAD8, CAD9, CADH I, cinnamyl alcohol dehydrogenase, cinnamyl alcohol dehydrogenase 1, cinnamyl alcohol dehydrogenase 12, cinnamyl alcohol dehydrogenase 2, cinnamyl alcohol dehydrogenase 3, cinnamyl alcohol dehydrogenase 4, cinnamyl alcohol dehydrogenase 5, cinnamyl alcohol dehydrogenase 7, cinnamyl alcohol dehydrogenase 9, cinnamyl alcohol dehydrogenase C, cinnamyl alcohol dehydrogenases, CtCAD1, CtCAD2, CtCAD3, dehydrogenase, cinnamyl alcohol, FC1, FLEXIBLE CULM1, HcCAD1, HcCAD2, LlCAD2, LtuCAD1, More, Mt-CAD1, Mt-CAD2, PhCAD1, PhCAD2, PhCAD3, PhCAD4, PtoCAD1, PtoCAD12, PtoCAD2, PtoCAD3, PtoCAD5, PtoCAD6, PtoCAD7, PtoCAD8, PtoCAD9, ScAdh6p, TaCAD12
ECTree
1.1.1.195 cinnamyl-alcohol dehydrogenaseAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cu2+
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activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+
EDTA
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activates at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
additional information
Zn2+
ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
zinc-type enzyme, ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
required, the enzyme contains the Zn-1 binding domain motif GHE(X)2G(X)5G(X)2V and the conserved Zn-1 catalytic residues C47, H69, and C163
Zn2+
required, Zn1 binding sequence is located at amino acid residues 68-82, and Zn2 binding sequence is located at amino acid residues 88-113
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 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
Zn2+
required, motif for both Zn2+ binding, modelling
Zn2+
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restores activity after incubation in buffer containing a divalent-cation exchange resin
Zn2+
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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
