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Information on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase and Organism(s) Arabidopsis thaliana and UniProt Accession P48523
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1.1.1.195 cinnamyl-alcohol dehydrogenaseIUBMB Comments
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
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Word Map
- 1.1.1.195
- lignin
-
lignification
- monolignols
-
phenylpropanoids
-
sinapyl
- 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
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
cinnamyl alcohol dehydrogenase, cad11, cinnamyl-alcohol dehydrogenase, cinnamyl alcohol dehydrogenases, scadh6p, tacad12, atcad4, cad10, ptocad1, cinnamyl alcohol dehydrogenase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Brown-midrib 1 protein
-
-
-
-
CAD
CAD 7/8
-
-
-
-
CAD2
-
-
-
-
cinnamyl alcohol dehydrogenase
dehydrogenase, cinnamyl alcohol
-
-
-
-
additional information
the enzyme belongs to the CAD protein family
CAD
-
-
-
-
cinnamyl alcohol dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
catalytic reaction mechanism, substrate and cofactor binding structure
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
catalytic reaction mechanism, substrate and cofactor binding structure
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
cinnamyl-alcohol:NADP+ oxidoreductase
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
CAS REGISTRY NUMBER
COMMENTARY
55467-36-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
-
-
r
additional information
?
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
?
additional information
?
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
-
substrate specificity of isozyme CAD4
-
-
?
additional information
?
-
role of the enzyme in lignin biosynthesis and structure formation
-
-
?
additional information
?
-
substrate specificity of isozyme CAD5
-
-
?
additional information
?
-
substrate specificity of isozyme CAD5
-
-
?
additional information
?
-
-
substrate specificity of isozyme CAD5
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
additional information
?
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
?
additional information
?
-
role of the enzyme in lignin biosynthesis and structure formation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
cofactor binding site structure determination and analysis
NADPH
cofactor binding site structure determination and analysis
NADP+
cofactor binding site structure determination and analysis
NADPH
cofactor binding site structure determination and analysis
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
zinc-type enzyme, ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
Zn2+
ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
enzyme expression pattern of AtCAD-C and AtCAD-D, no expression in silique
-
isoforms Cad-4, Cad-5, expression in root caps. Isoforms Cad-2, Cad-3, expression in non-lignifying root tips
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
hydroxycinnamaldehyde content is a more important determinant of digestibility than lignin content
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CADH4_ARATH
365
0
39098
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
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
additional information
additional information
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size
additional information
-
construction of a cad-c-cad-d-double mutant, which shows delayed vegetative growth and bolting, combined with reduced size
additional information
construction of 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
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
downregulation of (hydroxy)cinnamyl alcohol dehydrogenase (CAD) genes is another promising strategy to increase cell wall digestibility for biofuel production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sibout, R.; Eudes, A.; Pollet, B.; Goujon, T.; Mila, I.; Granier, F.; Seguin, A.; Lapierre, C.; Jouanin, L.
Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants
Plant Physiol.
132
848-860
2003
Arabidopsis thaliana (Q02971)
Youn, B.; Camacho, R.; Moinuddin, S.G.; Lee, C.; Davin, L.B.; Lewis, N.G.; Kang, C.
Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4
Org. Biomol. Chem.
4
1687-1697
2006
Arabidopsis thaliana (O49482), Arabidopsis thaliana (P48523), Arabidopsis thaliana
Sibout, R.; Eudes, A.; Mouille, G.; Pollet, B.; Lapierre, C.; Jouanin, L.; Seguin, A.
Cinnamyl alcohol dehydrogenase-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis
Plant Cell
17
2059-2076
2005
Arabidopsis thaliana (P48523), Arabidopsis thaliana
Eudes, A.; Pollet, B.; Sibout, R.; Do, C.T.; Seguin, A.; Lapierre, C.; Jouanin, L.
Evidence for a role of AtCAD 1 in lignification of elongating stems of Arabidopsis thaliana
Planta
225
23-39
2006
Arabidopsis thaliana (Q02971), Arabidopsis thaliana
Chen, A.P.; Zhong, N.Q.; Qu, Z.L.; Wang, F.; Liu, N.; Xia, G.X.
Root and vascular tissue-specific expression of glycine-rich protein AtGRP9 and its interaction with AtCAD5, a cinnamyl alcohol dehydrogenase, in Arabidopsis thaliana
J. Plant Res.
120
337-343
2007
Arabidopsis thaliana
Jourdes, M.; Cardenas, C.L.; Laskar, D.D.; Moinuddin, S.G.; Davin, L.B.; Lewis, N.G.
Plant cell walls are enfeebled when attempting to preserve native lignin configuration with poly-p-hydroxycinnamaldehydes: evolutionary implications
Phytochemistry
68
1932-1956
2007
Arabidopsis thaliana
Kim, S.J.; Kim, K.W.; Cho, M.H.; Franceschi, V.R.; Davin, L.B.; Lewis, N.G.
Expression of cinnamyl alcohol dehydrogenases and their putative homologues during Arabidopsis thaliana growth and development: lessons for database annotations?
Phytochemistry
68
1957-1974
2007
Arabidopsis thaliana
Lee, C.; Bedgar, D.L.; Davin, L.B.; Lewis, N.G.
Assessment of a putative proton relay in Arabidopsis cinnamyl alcohol dehydrogenase catalysis
Org. Biomol. Chem.
11
1127-1134
2013
Arabidopsis thaliana (O49482), Arabidopsis thaliana
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
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