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Enzyme Nomenclature
Information on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.195
Word Map on EC 1.1.1.195
- 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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coniferyl
- xylem
- coniferaldehyde
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ammonia-lyase
- sinapaldehyde
- cinnamoyl-coa
- populus
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guaiacyl
- eucalyptus
- cinnamaldehydes
- poplar
- agriculture
- taeda
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linum
- gunnii
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4.3.1.5
- podophyllotoxin
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cinnamoyl
- tremula
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syringyl
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hydroxycinnamyl
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loblolly
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p-coumaryl
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cadherin-11
- biofuel production
- synthesis
- industry
- 4-coumarate
- nutrition
- biotechnology
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thioacidolysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.195
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RECOMMENDED NAME
GeneOntology No.
cinnamyl-alcohol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
A-specific enzyme
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
A-specific enzyme; ordered bi-bi mechanism
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
acts stereospecifically on the pro-R-hydrogen atom of coniferyl alcohol
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
active site structure
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cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
catalytic reaction mechanism, substrate and cofactor binding structure; catalytic reaction mechanism, substrate and cofactor binding structure
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
random mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Fxcad1; cv. Chandler, octaploid cultivar, gene Fxcad1 and Fxcad2
SwissProt
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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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
TaCAD12 belongs to IV group in CAD family, phylogenetic analysis
evolution
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purified CAD by MALDI-TOF shows a significant homology to alcohol dehydrogenases of MDR superfamily
evolution
flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
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; 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
LtuCAD is a member of a multigene family that belongs to the medium-chain dehydrogenase/reductase superfamily. Sequence identity and similarity among Arabidopsis thaliana and Liriodendron tulipifera CAD protein homologues, overview
evolution
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties; 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
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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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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
knock-down of TaCAD12 transcript significantly represses resistance of the gene-silenced wheat plants to sharp eyespot caused by Rhizoctonia cerealis, whereas TaCAD12 overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot. Certain defense genes (Defensin, PR10, PR17c, and Chitinase1) and monolignol biosynthesis-related genes (TaCAD1, TaCCR, and TaCOMT1) are upregulated in the TaCAD12-overexpressing wheat plants but downregulated in TaCAD12-silencing plants
malfunction
loss of function of cinnamyl alcohol dehydrogenase 1 leads to unconventional lignin and a temperature-sensitive growth defect in Medicago truncatula. Insertion mutants Medicago truncatula show reduced lignin autofluorescence under UV microscopy and red coloration in interfascicular fibers. The phenotype is caused by insertion of retrotransposons into a gene annotated as encoding cinnamyl alcohol dehydrogenase, CAD1. NMR analysis indicates that the lignin is derived almost exclusively from coniferaldehyde and sinapaldehyde and is therefore strikingly different from classical lignins, which are derived mainly from coniferyl and sinapyl alcohols. Despite such a major alteration in lignin structure, the plants appear normal under standard conditions in the greenhouse or growth chamber.The plants are dwarfed when grown at 30°C. Glycome profiling reveals an increased extractability of some xylan and pectin epitopes from the cell walls of the cad1-1 mutant but decreased extractability of others, suggesting that aldehyde-dominant lignin significantly alters cell wall structure
malfunction
CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting
malfunction
disruption of the genes encoding both cinnamyl alcohol dehydrogenases (CADs), including CADC and CADD, in Arabidopsis thaliana results in the atypical incorporation of hydroxycinnamaldehydes into lignin. The cadc/cadd-deficient and ferulic acid hydroxylase1 (fah1) cadc/cadd-deficient plants are similar in growth to wild-type plants even though their lignin compositions are drastically altered. In contrast, disruption of CAD in the F5H-overexpressing background results in dwarfism. The dwarfed phenotype observed in these plants does not appear to be related to collapsed xylem, a hallmark of many other lignin-deficient dwarf mutants. Mutant cadc/cadd-deficient and fah1 cadc/cadd-deficient, and cadd-deficient-F5H-overexpressing plants have increased enzyme-catalyzed cell wall digestibility
malfunction
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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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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
A0A0U1ZF25;, D9ZKR7;
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; 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 is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
metabolism
enzyme CAD catalyzes the final step in monolignol biosynthesis, leading to lignin formation in plants
metabolism
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cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis 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
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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
the change in lignin content has some linear correlation with the expression level of isoform CAD1 mRNA in different tissues
physiological function
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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
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
enzyme CAD plays a role in defense responses to necrotrophic or soil-borne pathogens in wheat; enzyme overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot caused by the necrotrophic fungus Rhizoctonia cerealis
physiological function
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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
the enzyme plays a role in lignin biosynthesis and the defencedefence of abiotic stresses; the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defencedefence of abiotic stress in Plagiochasma appendiculatum; the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defence of abiotic stress in Plagiochasma appendiculatum
physiological function
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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
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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
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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
isozymes PtoCAD1, -2, and -8 function differently depending on the cellular environment; isozymes PtoCAD1, -2, and -8 function differently depending on the cellular environment; isozymes PtoCAD1, -2, and -8 function differently depending on the cellular environment; PtoCAD9 expression is very high in the bud, suggesting that it might be related to bud development
physiological function
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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; 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; 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; 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; CmCAD4 may be a pseudogene
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
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enzyme molecular docking analysis with substrates, active site structure, structure comparisons between isozymes, overview
additional information
lignin and sugar content and composition during stem development, overview; lignin and sugar content and composition during stem development, overview
additional information
lignin and sugar content and composition during stem development, overview; lignin and sugar content and composition during stem development, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview; enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
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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; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
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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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; 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; 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; 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; 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; 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; 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; 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; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis; residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dimethylcinnamyl alcohol + NADP+
2,4-dimethylcinnamaldehyde + NADPH
-
-
-
-
2-propanol + NADP+
? + NADPH + H+
-
2-propanol can be also used in the cofactor recycling catalytic system as co-solvent like ethanol, but at the same time cinnamaldehyde conversion is lower (85%) and cinnamyl alcohol production is accordingly lower
-
-
-
3,4-methylenedioxycinnamyl alcohol + NADP+
3,4-methylenedioxycinnamaldehyde + NADPH
-
-
-
-
3-methoxybenzylalcohol + NADP+
3-methoxybenzaldehyde + NADPH
-
-
-
-
4-bromocinnamyl alcohol + NADP+
4-bromocinnamaldehyde + NADPH
-
-
-
-
4-chlorocinnamyl alcohol + NADP+
4-chlorocinnamaldehyde + NADPH
-
-
-
-
4-coumaraldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
-
-
-
?
4-methoxybenzylalcohol + NADP+
4-methoxybenzaldehyde + NADPH
-
-
-
-
4-methoxycinnamyl alcohol + NADP+
4-methoxycinnamaldehyde + NADPH
-
-
-
-
4-methylcinnamyl alcohol + NADP+
4-methylcinnamaldehyde + NADPH
-
-
-
-
5-hydroxyconiferyl aldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
-
-
?
5-hydroxyconiferyl aldehyde + NADPH
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
5-hydroxyconiferyl aldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
-
-
-
r
5-hydroxyconiferylaldehyde + NADP+
5-hydroxyconiferyl alcohol + NADPH + H+
very low activity
-
-
?
5-hydroxyconiferylaldehyde + NADPH + H+
5-hydroxyconiferyl alcohol + NADP+
lowest catalytic efficiency
-
-
?
benzaldehyde + NADP+
benzoic acid + NADPH
-
the enzyme also shows dismutase activity
-
-
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
CAD4 displays slight activity for benzoyl alcohol
-
-
?
benzyl alcohol + NADP+
benzylaldehyde + NADPH + H+
slight activity
-
-
r
caffeyl aldehyde + NADPH
caffeyl alcohol + NADP+
-
-
-
r
caffeylaldehyde + NADP+
caffeyl alcohol + NADPH + H+
low activity
-
-
?
caffeylaldehyde + NADPH + H+
caffeyl alcohol + NADP+
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH + H+
-
-
-
?
cinnamyl aldehyde + NADPH
cinnamyl alcohol + NADP+
-
-
-
r
coumaryl alcohol + NADP+
coumaraldehyde + NADPH + H+
-
-
-
?
coumaryl aldehyde + NADPH + H+
coumaryl alcohol + NADP+
-
-
-
r
p-coumarylaldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
?
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
-
-
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
r
3,4-dimethoxycinnamyl alcohol + NADP+
3,4-dimethoxycinnamaldehyde + NADPH
-
-
-
-
-
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
catalytic preference for 4-coumaraldehyde
-
-
?
4-coumarylaldehyde + NADPH + H+
4-coumaryl alcohol + NADP+
high catalytic efficiency
-
-
?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
cofactor recycling catalytic system in which ADH reduces cinnamaldehyde to cinnamyl alcohol (oxidizing NADH to NAD+). THe NAD+ produced is then recycled by ADH at expense of ethanol, which acts as co-solvent for both substrate and product, and is present in large excess to force the whole process toward cinnamaldehyde reduction. Also, elimination of the obtained dehydrogenation product acetaldehyde drives cinnamaldehyde reduction toward completion. 1-2 mM is the ideal starting cinnamaldehyde concentration
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
key enzyme in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
involved in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
-
-
r
cinnamyl alcohol + NADP+
cinnamaldehyde + NADPH + H+
-
100% activity with 1 mM cinnamyl alcohol, 116% activity with 10 mM cinnamyl alcohol, reaction catalyzed by unspecific alcohol dehydrogenase (EC 1.1.1.1)
61% activity with 0.1 mM cinnamaldehyde, 7% activity with 1 mM cinnamaldehyde
-
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
favourite substrate
-
-
?
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
-
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4. Activity of Bmr6 is 2.5- and 34fold higher than CAD4 for coniferyl and sinapyl aldehyde, respectively
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4. Bmr6 activity is 2.2- and 2.6-fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates. Activity of Bmr6 is 2.5- and 34fold higher than CAD4 for coniferyl and sinapyl aldehyde, respectively
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
-
recombinant enzyme encoded by gene GH2
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
the forward reaction is the physiological reaction
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
?
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
low activity
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
best substrate
-
-
r
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
-
-
-
r
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4
-
-
?
coumaryl alcohol + NADP+
coumaryl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
r
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
?
p-coumaryl aldehyde + NADPH + H+
p-coumaryl alcohol + NADP+
-
-
-
r
sinapaldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Bmr6 displays significantly greater activity in comparison to CAD4
-
-
?
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Bmr6 activity is 2.2- and 2.6fold greater respectively, when coumaryl and sinapyl alcohols are used as substrates compared to coniferyl alcohol as a substrate
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
preferred substrate
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
recombinant enzyme encoded by gene GH2
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
low activity
-
-
?
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
very low activity
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
Brm6 has higher activities for the coniferyl and sinapyl aldehydes in comparison to the corresponding alcohols
-
-
r
additional information
?
-
-
32 single nucleotide polymorphisms in the coding region of CAD, whereby 12 are nonsynonymous mutations and 20 are synonymous mutations. 11 and three synonymous mutations are detected in Acacia auriculiformis A3 x Acacia mangium M22 and Acacia auriculiformis A6 x Acacia mangium M20 parental combination, respectively. The synonymous mutations detected are 20 in both genes. The high occurences of single nucleotide polymorphisms are possible because the plant has to adopt physiologically to a variety of unpredictable environmental conditions
-
-
-
additional information
?
-
-
32 single nucleotide polymorphisms in the coding region of CAD, whereby 12 are nonsynonymous mutations and 20 are synonymous mutations. 11 and three synonymous mutations are detected in Acacia auriculiformis A3 x Acacia mangium M22 and Acacia auriculiformis A6 x Acacia mangium M20 parental combination, respectively. The synonymous mutations detected are 20 in both genes. The high occurences of single nucleotide polymorphisms are possible because the plant has to adopt physiologically to a variety of unpredictable environmental conditions
-
-
-
additional information
?
-
role of the enzyme in lignin biosynthesis and structure formation
-
-
-
additional information
?
-
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
-
additional information
?
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
-
additional information
?
-
-
substrate specificity of isozyme CAD4
-
-
-
additional information
?
-
substrate specificity of isozyme CAD4
-
-
-
additional information
?
-
substrate specificity of isozyme CAD4
-
-
-
additional information
?
-
-
substrate specificity of isozyme CAD5
-
-
-
additional information
?
-
substrate specificity of isozyme CAD5
-
-
-
additional information
?
-
substrate specificity of isozyme CAD5
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
substituted and unsubstituted benzaldehydes
-
-
-
additional information
?
-
-
enzyme involved in lignification in vascular plants
-
-
-
additional information
?
-
-
not: methanol, ethanol, n-propanol, n-butanol, isobutanol, geraniol, various aromatic alcohols (e.g. salicyl alcohol, vanillyl alcohol, piperonyl alcohol)
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
coniferylaldehyde and sinapylaldehyde are the preferred substrates
-
-
-
additional information
?
-
coniferylaldehyde and sinapylaldehyde are the preferred substrates
-
-
-
additional information
?
-
-
no activity with methanol and ethanol as alcoholic substrates
-
-
-
additional information
?
-
the enzyme shows broad substrate specificity, LlCAD2 shows significant activity against cinnamyl substrates, but is almost inactive against aliphatic and other benzyl compounds. Possible involvement of histidine at the active site. Low activity with benzaldehyde, anisaldehyde, vanillin, and syringaldehyde. No or very poor activity with formaldehyde, acetaldehyde, propionaldehyde, and butryaldehyde
-
-
-
additional information
?
-
-
the enzyme shows broad substrate specificity, LlCAD2 shows significant activity against cinnamyl substrates, but is almost inactive against aliphatic and other benzyl compounds. Possible involvement of histidine at the active site. Low activity with benzaldehyde, anisaldehyde, vanillin, and syringaldehyde. No or very poor activity with formaldehyde, acetaldehyde, propionaldehyde, and butryaldehyde
-
-
-
additional information
?
-
-
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
the enzyme Mt-CAD2 shows low activity with all substrates and compared to the activities of Mt-CAD1, substrate binding and specificity of Mt-CAD2, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
FC1 plays an important role in the biosynthesis of lignin and the control of culm strength in rice, especially in the first internodes, and FC1 deficiency in the first internodes is the main cause of the lodging trait in fc1 plants. FC1 mutant exhibits an abnormal development phenotype, including late heading time, semi-dwarf habit, and causes a reduction in cell wall thickness, as well as a decrease in lignin. Extracts from the first internodes and panicles of FC1 plants exhibit drastically reduced cinnamyl-alcohol dehydrogenase activity. Overexpression of FC1 does not affect the cell wall composition
-
-
-
additional information
?
-
-
not: sinapaldehyde, 4-hydroxybenzaldehyde, vanillin, 4-hydroxy-3,5-dimethoxybenzaldehyde, 3,4-dimethoxybenzaldehyde, salicylaldehyde, 2-methoxybenzaldehyde, mannose, acetaldehyde
-
-
-
additional information
?
-
-
final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
-
-
-
additional information
?
-
beta-glucuronidase expression driven by the CAD promoter is wound-inducible
-
-
-
additional information
?
-
-
beta-glucuronidase expression driven by the CAD promoter is wound-inducible
-
-
-
additional information
?
-
-
liginification and lignin topochemistry indifferent samples, overview
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
KJ159967;
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
PtoCAD3 has poor affinity for both substrates and is active only at high substrate concentrations
-
-
-
additional information
?
-
-
CAD4 and CAD10 possess transcription factor binding motifs involved in development and in response to various stresses. CAD1, CAD2, CAD10, and CAD11 possess promoter motifs involved in the response to fungal elicitors. CAD2, CAD4, CAD5, CAD7, CAD9, rCAD10 and CAD16 possess motifs involved in response to wounding, herbivore stress, as well as other stresses
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
-
-
-
additional information
?
-
a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
-
-
-
additional information
?
-
-
a C-to-T transition mutation is present in bmr6 but not in any wild-type sequence. This mutation changes amino acid 132 of the protein from Gln (CAG) to a stop codon (UAG). The bmr6 sequence encodes a predicted truncated protein that lacks the nucleotide binding (NADPH) and C-terminal catalytic domains, thus bmr6 is presumably a null allele. No activity with caffeoyl alcohol and benzoyl alcohol
-
-
-
additional information
?
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
-
CAD4 expression is significantly increased in bmr6 and bmr6 bmr12 plants relative to the wild-type and bmr12, 5- and 2.5fold, respectively, which may highlight a compensatory mechanism for loss of CAD activity in bmr6. No activity with caffeoyl alcohol
-
-
-
additional information
?
-
-
CAD is one of the enzymes involved in monolignol biosynthesis, which is critically important for host defence against both appropriate and inappropriate pathogen invasion in wheat
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
O49482, P48523
-
-
-
r
coniferaldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
isoform CAD3 has a higher binding preference with coniferaldehyde over sinapaldehyde, followed by isoforms CAD4, CAD2, and CAD1, respectively
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
Q9ATW1
key enzyme in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH
cinnamyl alcohol + NADP+
-
involved in lignin biosynthesis
-
-
?
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
U3TDQ6, U3TH11, U3TI46
-
-
-
r
cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
A0A0U1ZF25, D9ZKR7
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
the enzyme is involved in lignin synthesis and increases concomitantly with cell differentiation
-
-
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Q02971
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
P48523
coniferyl alcohol is converted into its corresponding aldehyde during lignin biosynthesis
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
B5AR58
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Q1HGA8
-
-
-
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
A0A1D6BJ11
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
O49482, P48523
-
-
-
r
coniferyl aldehyde + NADPH
coniferyl alcohol + NADP+
Q5D4P8, Q5D4P9
CAD1 and CAD2 are involved in biosynthesis of coniferyl alcohol in Nicotiana tabacum
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
U3TDQ6, U3TH11, U3TI46
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
A0A0U1ZF25, D9ZKR7
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
the forward reaction is the physiological reaction
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
A0A023RBJ1, KJ159967, T1WUT6, T1WUU2, T1WVG5, T1WW77, T1WW82, T1WWB9, T1WWR8
-
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
A0A023RBJ1, KJ159967, T1WUT6, T1WUU2, T1WVG5, T1WW77, T1WW82, T1WWB9, T1WWR8
low activity
-
-
r
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
B5AR58
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Q1HGA8
-
-
-
r
p-coumaryl alcohol + NADP+
p-coumaryl aldehyde + NADPH + H+
Q1HGA8
-
-
-
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
Q1HGA8
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
U3TDQ6, U3TH11, U3TI46
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
A0A0U1ZF25, D9ZKR7
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
A0A023RBJ1, KJ159967, T1WUT6, T1WUU2, T1WVG5, T1WW77, T1WW82, T1WWB9, T1WWR8
-
-
-
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
A0A023RBJ1, KJ159967, T1WUT6, T1WUU2, T1WVG5, T1WW77, T1WW82, T1WWB9, T1WWR8
very low activity
-
-
r
additional information
?
-
Q02971
role of the enzyme in lignin biosynthesis and structure formation
-
-
-
additional information
?
-
-
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
-
additional information
?
-
P48523
the enzyme is involved in cell wall biosynthesis, phenylpropanoid pathway from phenylalanine to monolignols, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
enzyme involved in lignification in vascular plants
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
Q1HGA8
the enzyme is involved in moolignol and lignan biosynthesis, phenolic compound spectrum in control and elicited cells, overview
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
final step in a branch of phenylpropanoid synthesis specific for production of lignin monomers
-
-
-
additional information
?
-
-
liginification and lignin topochemistry indifferent samples, overview
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of monolignols, it is not rate-limiting for lignin production under physiologic conditions
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
additional information
?
-
-
one of the regulating enzymes which controls the formation of guaiacyl and syringyl lignins
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
cofactor binding site structure determination and analysis; cofactor binding site structure determination and analysis
NADP+
-
NADPH
-
dependent for, binding and specificity mechanism, interaction through Ser210, Arg211, and Lys215 and the terminal phosphate group
NADPH
cofactor binding site structure determination and analysis; cofactor binding site structure determination and analysis
NADPH
the NADPH binding sequence is located at amino acid residues 188-193; the NADPH binding sequence is located at amino acid residues 189-194; the NADPH binding sequence is located at amino acid residues 191-196
NADPH
; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling; motif for both NADPH binding modelling
additional information
the enzyme has a highly conserved Rossmann fold NAD(P)H/NAD(P)+ binding domain
-
additional information
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
additional information
-
the motif GLGGLG participates in binding the diophosphate group of NADP+
-
additional information
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
additional information
-
the enzyme is highly cofactor specific and is active only in presence of NADP(H), exhibiting insignificant activity with NAD(H) (up to 3 mM)
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
-
activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+
EDTA
-
activates at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
additional information
Zn2+
ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70; zinc-type enzyme, ligand binding structure, Zn2+ is bound in a tetrahedral coordination involving Glu70
Zn2+
required, the enzyme contains the Zn-1 binding domain motif GHE(X)2G(X)5G(X)2V and the conserved Zn-1 catalytic residues C47, H69, and C163
Zn2+
required, Zn1 binding sequence is located at amino acid residues 68-82, and Zn2 binding sequence is located at amino acid residues 88-113; required, Zn1 binding sequence is located at amino acid residues 69-83, and Zn2 binding sequence is located at amino acid residues 89-114; required, Zn1 binding sequence is located at amino acid residues 71-85, and Zn2 binding sequence is located at amino acid residues 91-116
Zn2+
A0A0U1ZF25;, D9ZKR7;
required; required, Zn1 binding sequence is GHE(X)2G(X)5G(X)2V located at amino acid residues 68-82, and Zn2 binding sequence GD(X)9,10C(X)2C(X)2(X)7C located at amino acid residues 88-114, structural zinc coordinated residue are Cys100, Cys103, Cys106, and Cys114
Zn2+
4 Zn2+ per homodimer, the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions
Zn2+
required; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling; required, motif for both Zn2+ binding, modelling
Zn2+
-
restores activity after incubation in buffer containing a divalent-cation exchange resin
Zn2+
-
required, Zn1-binding motif [GHE(X)2G(X)5G(X)2 V] and Zn2-binding motif [GD(X)9,10C(X)2C(X)2C(X)7C] occur in most of the isozymes, overview
Zn2+
require, the TaCAD12 protein contains one alcohol dehydrogenase domain (42-157 aa) with two Zn binding sites (41-63 and 76-90 aa) and one Zn-binding dehydrogenase domain (199-323 aa)
additional information
slight activating effect by KCl at 100 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-monophosphate
-
IC50: 1.58 mM with NADP+ and 0.74 mM with NAD+
cinnamaldehyde
-
substrate inhibition mediated by cinnamaldehyde concentrations far from the Km value of 0.46 mM, which does not allow for excessively increasing the starting cinnamaldehyde concentration, since the process yield may be greatly affected
coniferyl aldehyde
competitve, a stronger inhibitor than sinapyl aldehyde; competitve, a stronger inhibtior than sinapyl aldehyde; competitve, a stronger inhibtior than sinapyl aldehyde
Ni
-
CAD activity is not affected by concentrations up to 0.12 mM, phenolic metabolism is not substantially affected by Ni excess
RNAi
-
RNAi-mediated transient gene silencing in the epidermis leads to a higher penetration efficiency of Blumeria graminis f. sp. tritici (64%) than in the controls. Gene silencing also compromises penetration resistance to varying degrees with different genes against an inappropriate pathogen, Blumeria graminis f. sp. hordei. Co-silencing of CAD and other genes involved in monolignol biosynthesis leads to greater penetration of Blumeria graminis f. sp. tritici or Blumeria graminis f. sp. hordei than when the genes are silenced separately. Gene silencing hamperes host autofluorescence response at fungal contact sites
-
sinapyl aldehyde
competitve, a weaker inhibitor than coniferyl aldehyde; competitve, a weaker inhibtior than coniferyl aldehyde; competitve, a weaker inhibtior than coniferyl aldehyde
Zn2+
-
inhibitory at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
Zn2+
the enzyme is a Zn-metalloenzyme with 4 Zn2+ per dimer. The enzyme is inhibited in presence of externally supplemented Zn2+ ions, strong inhibition
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves results in reduced penetration resistance against Puccinia hordei infection
[[(2-hydroxyphenyl) amino]sulphinyl] acetic acid, 1.1 dimethyl ester
-
inhibition of cinnamyl alcohol dehydrogenase activity. Treatment of leaves has no efffect in on resistance against Puccinia hordei infection
additional information
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
additional information
-
poor inhibition by Triton X-100 and Tween 80 at 1%, and by glucose at 20%
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO2
-
high CO2 stimulates progressively the enzyme, as well as of other enzymes involved in metabolism of phenolic compounds, overview
jasmonate
accumulation of CAD mRNA in response to jasmonate application and mechanical wounding
additional information
-
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
the enzyme is induced in suspended cell by elicitors from Fusarium oxysporum and Botrytis cinerea, overview
-
additional information
-
Cinnamyl alcohol dehydrogenase activity remains unaffected by both methyl jasmonate and salicylic acid. This indicates that methyl jasmonate and salicylic acid induce the accumulation of phenolic compounds in ginseng root by altering the phenolic synthesis enzymes
-
additional information
-
the enzyme is not nduced by stress, but is related to cell wall lignification
-
additional information
-
mechanical stress application induces a strong increase of CAD activity in rubbed internode with an approximately 2fold increase when compared to control tomato internodes. Increased activity of CAD is associated with a higher lignin content in the rubbed internode
-
additional information
-
CAD transcripts are accumulated in response to infection with Blumeria graminis f. sp. tritici. Accumulates at 6 hpi, followed by a slight decrease at 12 hpi and then a sharp increase at 24 hpi
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0244
5-hydroxyconiferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0891
caffeoyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0042
coumaryl alcohol
pH not specified in the publication, temperature not specified in the publication
0.013
4-coumaraldehyde
wild-type, 30°C, pH not specified in the publication
0.036
4-coumaraldehyde
mutant D57A, 30°C, pH not specified in the publication
0.114
4-coumaraldehyde
mutant T49A, 30°C, pH not specified in the publication
0.117
4-coumaraldehyde
mutant H52A, 30°C, pH not specified in the publication
0.0382
4-coumarylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
0.1122
4-coumarylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
0.09318
5-hydroxyconiferylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
0.152
5-hydroxyconiferylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
31
benzaldehyde
-
pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+
0.06592
caffeylaldehyde
isoform CAD2, at pH 6.0 and 25°C
-
0.09463
caffeylaldehyde
isoform CAD1, at pH 6.0 and 25°C
-
0.03115
coniferaldehyde
isoform CAD2, at pH 6.0 and 25°C
0.08554
coniferaldehyde
isoform CAD1, at pH 6.0 and 25°C
0.00098
coniferyl alcohol
pH not specified in the publication, temperature not specified in the publication
0.0075
coniferyl alcohol
; pH 8.8, temperature not specified in the publication
0.117
coniferyl alcohol
; pH 8.8, temperature not specified in the publication
0.0038
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.0066
coniferyl aldehyde
-
wild-type Mt-CAD2, pH and temperature not specified in the publication
0.0068
coniferyl aldehyde
pH 6.5-7.5, 26°C, recombinant enzyme
0.0085
coniferyl aldehyde
-
Mt-CAD1, pH and temperature not specified in the publication
0.0109
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.01996
coniferyl aldehyde
pH 6.0, 30°C, recombinant His-tagged enzyme
0.02062
coniferyl aldehyde
pH 5.0, 30°C, recombinant His-tagged enzyme; pH 5.0, 30°C, recombinant His-tagged enzyme
0.0219
coniferyl aldehyde
pH not specified in the publication, temperature not specified in the publication
0.024
coniferyl aldehyde
pH 6.5-7.5, 30°C, recombinant enzyme
0.0289
coniferyl aldehyde
recombinant GST-tagged enzyme, pH and temperature not specified in the publication
0.031
coniferyl aldehyde