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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
CAD tends to exist in multi-gene families with one gene being primarily responsible for lignin biosynthesis. The BdCAD family consists of Bradi3g06480 (BdCAD1), Bradi3g17920 (BdCAD2), Bradi3g22980 (BdCAD3), Bradi4g29770 (BdCAD4), Bradi4g29780 (BdCAD5), Bradi5g04130 (BdCAD6), and Bradi5g21550 (BdCAD7)
evolution
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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
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enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1
evolution
flax CAD belongs to the bona-fide CAD family, phylogenetic analysis
evolution
LtuCAD is a member of a multigene family that belongs to the medium-chain dehydrogenase/reductase superfamily. Sequence identity and similarity among Arabidopsis thaliana and Liriodendron tulipifera CAD protein homologues, overview
evolution
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties
evolution
nine CAD/CAD-like genes in Populus tomentosa are classified into four classes based on expression patterns, phylogenetic analysis and biochemical properties. Isozyme PtoCAD12 is the only protein in the group III, as it is distinct from other PtoCADs and closely related to PoptrCAD12, AtCAD1 and OsCAD1
evolution
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purified CAD by MALDI-TOF shows a significant homology to alcohol dehydrogenases of MDR superfamily
evolution
TaCAD12 belongs to IV group in CAD family, phylogenetic analysis
evolution
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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
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
knock-down of TaCAD12 transcript significantly represses resistance of the gene-silenced wheat plants to sharp eyespot caused by Rhizoctonia cerealis, whereas TaCAD12 overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot. Certain defense genes (Defensin, PR10, PR17c, and Chitinase1) and monolignol biosynthesis-related genes (TaCAD1, TaCCR, and TaCOMT1) are upregulated in the TaCAD12-overexpressing wheat plants but downregulated in TaCAD12-silencing plants
malfunction
loss of function of cinnamyl alcohol dehydrogenase 1 leads to unconventional lignin and a temperature-sensitive growth defect in Medicago truncatula. Insertion mutants Medicago truncatula show reduced lignin autofluorescence under UV microscopy and red coloration in interfascicular fibers. The phenotype is caused by insertion of retrotransposons into a gene annotated as encoding cinnamyl alcohol dehydrogenase, CAD1. NMR analysis indicates that the lignin is derived almost exclusively from coniferaldehyde and sinapaldehyde and is therefore strikingly different from classical lignins, which are derived mainly from coniferyl and sinapyl alcohols. Despite such a major alteration in lignin structure, the plants appear normal under standard conditions in the greenhouse or growth chamber.The plants are dwarfed when grown at 30°C. Glycome profiling reveals an increased extractability of some xylan and pectin epitopes from the cell walls of the cad1-1 mutant but decreased extractability of others, suggesting that aldehyde-dominant lignin significantly alters cell wall structure
malfunction
transgenic silencing of BdCAD1 causes altered flowering time and increases stem count and weight. Downregulation of BdCAD1 causes a leaf brown midrib phenotype. While acetyl bromide soluble lignin measurements are equivalent in BdCAD1 downregulated and control plants, histochemical staining and thioacidolysis indicate a decrease in lignin syringyl units and reduced syringyl/guaiacyl ratio in the transgenic plants. The perturbed enzyme results in greater stem biomass yield and bioconversion efficiency
malfunction
enzyme downregulation or knockout causes a reduction of lignin, which leads to severe plant dwarfism and a decreased biomass as well as decreased plant resistance to pathogens
malfunction
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enzyme downregulation results in a significant decrease in both elastic modulus and yield stress while wood density and cellulose microfibril angle are not affected. Enzyme-downregulated poplars show increased incorporation of hydroxycinnamaldehydes. Enzyme downregulation results in red xylem tissue
malfunction
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isoform CAD2 downregulation improves saccharification efficiency. CAD2 enzyme-deficient mutants accumulate feruloyl and sinapoyl hexose conjugates. The total amount of lignin is reduced in the mutants, and only minor amounts of hydroxycinnamaldehydes are incorporated. Oligolignols composed of coniferyl and sinapyl alcohols are reduced, whereas those with one sinapaldehyde unit are increased in abundance in cad2 mutants
malfunction
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CAD downregulation does not disturb at all or has only slight effect on flax plants' development in vivo, while the resistance against flax major pathogen Fusarium oxysporum decreases slightly. The modification positively affects fibre possessing, it results in more uniform retting
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metabolism
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cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
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cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis
metabolism
cinnamyl alcohol dehydrogenase (CAD) is a key enzyme in lignin biosynthesis and catalyzes the final step in the synthesis of monolignols
metabolism
cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase catalyze key steps in the pathway of lignin monomer biosynthesis
metabolism
cinnamyl alcohol dehydrogenase is a key enzyme in the lignin biosynthesis, lignin biosynthesis pathway within the phenylpropanoid route, overview
metabolism
enzyme CAD catalyzes the final step in monolignol biosynthesis, leading to lignin formation in plants
metabolism
enzyme CAD is involved in the lignin biosynthesis. CAD converts cinnamylaldehyde to cinnamyl alcohol in the final step of the monolignol biosynthesis pathway and is a key enzyme in the pathway. The monolignol biosynthesis is the first major step in lignin biosynthesis, and crosslinkage of monolignols by perocidases and laccases is the second major step
metabolism
key enzyme in the biosynthesis of lignin. Artemisinin, arteannuin B, and other sesquiterpenes are profiled in the leaves of enzyme-overexpressing vs. wild-type plants
metabolism
the enzyme is responsible for lignin biosynthesis
metabolism
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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
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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
the change in lignin content has some linear correlation with the expression level of isoform CAD1 mRNA in different tissues
physiological function
enzyme overexpression markedly enhances resistance of the transgenic wheat lines to sharp eyespot caused by the necrotrophic fungus Rhizoctonia cerealis
physiological function
the enzyme plays a role in lignin biosynthesis and the defencedefence of abiotic stresses
physiological function
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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
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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
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. CAD3 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network
physiological function
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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. CmCAD1 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network
physiological function
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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. CmCAD5 is involved in the lignin biosynthesis induced by both abiotic and biotic stresses and in tissue-specific developmental lignification through a CAD genes family network, CmCAD5 may also function in flower development
physiological function
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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
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
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CmCAD4 may be a pseudogene
physiological function
enzyme CAD plays a role in defense responses to necrotrophic or soil-borne pathogens in wheat
physiological function
hydroxycinnamaldehyde content is a more important determinant of digestibility than lignin content
physiological function
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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
isozymes PtoCAD1, -2, and -8 function differently depending on the cellular environment
physiological function
PtoCAD9 expression is very high in the bud, suggesting that it might be related to bud development
physiological function
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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
the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defence of abiotic stress in Plagiochasma appendiculatum
physiological function
the two PaCADs, PaCAD1 and PaCAD2, play twin roles in lignin biosynthesis and the defencedefence of abiotic stress in Plagiochasma appendiculatum
physiological function
When expressed in the Arabidopsis cad4 cad5 double mutant, LtuCAD1 is able to restore the total lignin content and decrease the S/G lignin ratio
physiological function
isoform CAD6 is involved in developmental lignification in rice and also plays a role in the defense response against rice pathogens
physiological function
isoforms CAD1 and 2 take part in the lignification of maturing stem and in the response to cold and drought stress
physiological function
isoforms CAD2 is involved in developmental lignification in rice and also plays a role in the defense response against rice pathogens
physiological function
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the enzyme is involved in lignification
physiological function
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the enzyme performs cadmium absorption and fixation to lignified cell wall during stress conditions. Enzyme-overexpressing plants exhibit higher cadmium tolerance compared to the wild type with higher chlorophyll and proline contents and antioxidant enzyme activity, as well as a lower methane dicarboxylic aldehyde content, electric conductivity and reactive oxygen species when exposed to cadmium stress due to a lower amount of Cd distributed in the cytoplasm
additional information
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enzyme molecular docking analysis with substrates, active site structure, structure comparisons between isozymes, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling and molecular docking, substrate binding pocket structure, overview
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
KJ159967
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
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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
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
KJ159967
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
enzyme structure modelling, overview. Residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis, except for residue C58 in PtoCAD1
additional information
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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, except for residue C58 in PtoCAD1
additional information
lignin and sugar content and composition during stem development, overview
additional information
lignin and sugar content and composition during stem development, overview
additional information
only BdCAD1 contains both active substrate binding residues, W119 and F298, which determine specificity for aromatic alcohols, and the conserved S212 residue that determines NADP(H) binding at that position
additional information
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only BdCAD1 contains both active substrate binding residues, W119 and F298, which determine specificity for aromatic alcohols, and the conserved S212 residue that determines NADP(H) binding at that position
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
KJ159967
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
residues T49, Q53, L58, M60, C95, W119, V276, P286, M289, L290, F299, and I300 are conserved and putatively involved in catalysis
additional information
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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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the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Mmolecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, structural modeling of Mt-CAD1, overview
additional information
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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. 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