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evolution
phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
evolution
the conserved motifs G-X-X-G-X-X-A and D-X-X-D are reported to be involved in NAD(P) binding and adenine binding pocket stabilization. In addition, the NADP specificity motif R(X)5K is identified, which is a key structure that distinguishes CCR from other NAD(H)-dependent SDRs. Sequence comparisons and phylogenetic analysis of Populus tometosa CCRs, overview. Of the 11 PtoCCR and PtoCCR-like proteins, PtoCCR1 and 7 each catalyze at least one substrate. PtoCCR1 is active only with feruloyl-CoA as a substrate, while PtoCCR7 accepts all hydroxycinnamoyl-CoA esters
evolution
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phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
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malfunction
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Ccr1 knockout mutants exhibit a dramatic decrease in S lignin in vascular tissue
malfunction
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in the ccr1 mutant, CCR1 gene expression is reduced to 31% of the residual wild type level leading to a decrease in lignin content and significant changes in lignin structure. 4-hydroxyphenyl units are strongly decreased and the syringyl/guaiacyl ratio is slightly increased. Down-regulation of CCR1 alters schlerenchymatic fibre morphology and cell wall structure. Moderate down-regulation of CCR1 significantly improves cell wall digestibility in maize
malfunction
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20 month-old trees transgenic trees with downregulated CCR enzymes show up to 161% increased ethanol yield from tissues including bark, generated from the lignocellulosic biomass, strong downregulation of CCR also affects biomass yield. Wood samples derived from the transgenic trees are more easily processed into ethanol than wild-type. The improved saccharification yield is due to a higher cellulose conversion and correlates with the abundance of ferulic acid markers
malfunction
AtCCR2 expression is increased in Arabidopsis ccr1 mutant and function is partly compensated
malfunction
Betula platyphylla x Betula pendula
BpCCR1 overexpression increases lignin content up to 14.6%, and its suppression decreases lignin content by 6.3%. Modification of BpCCR1 expression leads to conspicuous changes in wood characteristics, including xylem vessel number and arrangement, and secondary wall thickness. The growth of transgenic trees in terms of height is also significantly influenced by the modification of BpCCR1 genes. The secondary xylem microstructures of stems base is altered with thicker cell walls of xylem fibers, penotype, overview
malfunction
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ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
malfunction
levels of G-monomers are considerably reduced in FaCCR-silenced fruits. Phenotypic analysis shows that the texture of the fruits injected with different FaCCR constructs is more solid than that of the untreated fruits , but up- or downregulation of the enzyme does not alter the red color and appearance of the fruits
malfunction
T154Y mutation in SbCCR1 leads to broader substrate specificity and faster turnover
malfunction
the positively charged extended structure of His208 was important in stabilizing CoA, while the mutants (M208, V208, and Y208) were unable to assume this function
malfunction
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enzyme downregulation increases the biosynthesis of phenolic acids
malfunction
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enzyme knockdown transgenics display a decrease in root and anther lignin depositions. Isoform CCR14 knockdown transgenics display loss of lignification in their anthers
malfunction
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suppression of enzyme gene expression results in a reduction in cinnamyl alcohol dehydrogenase enzyme activity in stem-differentiating xylem
malfunction
truncated enzyme lines (CCR-3, CCR-7 and CCR-12) show marked reduction in guaiacyl lignin which is reduced by 10.2% in both CCR-3 and CCR-7, and 9.3% in CCR-12. The down-regulation of lignin leads to significant increase in total phenolics content than the wild type control
malfunction
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ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
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metabolism
the enzyme carries out the first committed step in monolignol biosynthesis and acts as a first regulatory point in lignin formation
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
cinnamoyl-CoA reductase (CCR) is the first enzyme in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis. It is likely that Mt-CCR1 is the major CCR isozyme involved in lignin biosynthesis, and Mt-CCR2 is proposed to be involved in an alternative route for S lignin biosynthesis in Medicago truncatula
metabolism
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enzyme cinnamoyl-CoA reductase (CCR) catalyzes the first step in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
Betula platyphylla x Betula pendula
the enzyme is a key enzyme involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in lignin biosynthesis
metabolism
the enzyme is involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in the Monolignol biosynthetic pathway in dicotyledonous angiosperms, pathway overview
metabolism
the enzyme is involved in the the monolignol biosynthetic pathway
metabolism
the formation of 4-hydroxycinnamaldehydes is catalyzed by 4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR). 4-Hydroxycinnamaldehydes are a class of natural plant secondary products that includes coniferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffealdehyde. They are involved in several secondary metabolism pathways, such as those involved in the biosynthesis of phenolic acids, monolignols, flavonoids and terpenoids. 4-Hydroxycinnamaldehydes are also key intermediates in the biosynthesis and degradation of lignins, which protect cell wall polysaccharides from microbial degradation
metabolism
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
metabolism
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cinnamoyl CoA reductase is the dedicated enzyme in the lignin pathway
metabolism
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isoform CCR14 is a substrate of the SCF(FBK1) E3 ligase complex, and its degradation is mediated by the 26S proteasome
physiological function
CCR is responsible for the CoA ester conversion into aldehyde in monolignol biosynthesis, which diverts phenylpropanoid-derived metabolites into the biosynthesis of lignin. Lignifications in blueberry fruits are regulated under various post-harvest conditions
physiological function
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cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
physiological function
cinnamoyl-CoA reductase catalyzes the reduction of cinnamoyl-CoA esters to their respective cinnamaldehydes and is considered as a key enzyme in lignin formation
physiological function
cinnamoyl-coenzyme A reductase (CCR) catalyzes the reduction of hydroxycinnamoyl-CoA esters using NADPH to produce hydroxycinnamyl aldehyde precursors in lignin synthesis. Isozyme SbCCR2 displays greater activity toward 4-coumaroyl-CoA than does isozyme SbCCR1, which implies a role in the synthesis of defense-related lignin. CCR1 is involved in lignification of stem tissues, whereas CCR2 is involved in lignification in response to attack by pathogens
physiological function
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enzyme CCR is involved in lignin biosynthesis and might be playing a role in drought and salinity stress
physiological function
Betula platyphylla x Betula pendula
specific functions of a birch enzyme CCR1 in wood formation and growth
physiological function
the enzyme is involved in drought defense
physiological function
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isoform CCR20 is primarily involved in developmental deposition of lignins in secondary cell walls
physiological function
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vessel-specific reintroduction of isoform CCR1 in dwarfed ccr1 mutants restores vessel and xylary fiber integrity and increases biomass
physiological function
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cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
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additional information
active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
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active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
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structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
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structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
additional information
the substrate-binding domain of the SbCCR1 is surrounded by two groups of a-helices, and the floor of the substrate-binding pocket is largely composed of beta-strands. Residues T154 and Y310 ae involved in substrate binding with ferulic acid, Tyr310 binds the 4-hydroxyl of feruloyl-CoA, while Thr154 binds the 3-methoxy group of this molecule. Molecular docking and modelling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
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