1.2.1.44: cinnamoyl-CoA reductase
This is an abbreviated version!
For detailed information about cinnamoyl-CoA reductase, go to the full flat file.
Word Map on EC 1.2.1.44
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1.2.1.44
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lignin
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cinnamyl
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monolignols
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phenylpropanoids
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lignification
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xylem
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caffeoyl-coa
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p-coumaroyl-coa
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leucocephala
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ccoaomt
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leucaena
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4-coumarate:coa
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gunnii
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sinapoyl
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guaiacyl
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syringyl
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cinnamyl-alcohol
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coniferaldehyde
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sinapoyl-coa
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lignin-specific
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sinapaldehyde
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non-condensed
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thioacidolysis
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biotechnology
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synthesis
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industry
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agriculture
- 1.2.1.44
- lignin
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cinnamyl
- monolignols
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phenylpropanoids
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lignification
- xylem
- caffeoyl-coa
- p-coumaroyl-coa
- leucocephala
- ccoaomt
- leucaena
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4-coumarate:coa
- gunnii
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sinapoyl
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guaiacyl
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syringyl
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cinnamyl-alcohol
- coniferaldehyde
- sinapoyl-coa
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lignin-specific
- sinapaldehyde
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non-condensed
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thioacidolysis
- biotechnology
- synthesis
- industry
- agriculture
Reaction
Synonyms
AtCCR1, BpCCR1, CCR, CCR1, CCR12, CCR14 isoform, CCR17, CCR19, CCR2, CCR2-1, CCR20, CCR21, CCR3, CCR7, CCRH1, cinnamoyl CoA reductase, cinnamoyl CoA reductase 1, cinnamoyl coenzyme A reductase, cinnamoyl-Co-enzyme A reductase, cinnamoyl-CoA reductase, cinnamoyl-CoA reductase 1, cinnamoyl-CoA reductase1, cinnamoyl-CoA reductase2, cinnamoyl-CoA:NADPH reductase, cinnamoyl-coenzyme A reductase, cinnamoyl-coenzyme A reductase 1, FaCCR, feruloyl coenzyme A reductase, feruloyl-CoA reductase, ferulyl-CoA reductase, HcCCR1, HcCCR2, Ll-CCRH1, OsCCR1, p-hydroxycinnamoyl coenzyme A reductase, Ph-CCR1, PtCCR, PtoCCR1, PtoCCR7, PvCCR1, PvCCR2, reductase, cinnamoyl coenzyme A, SbCCR1, SbCCR2-1, SbCCR2-2, Ta-CCR2, VcCCR
ECTree
1.2.1.44 cinnamoyl-CoA reductaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.2.1.44 - cinnamoyl-CoA reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D77G
D77N
the mutant has same substrate affinity (feruloyl CoA) as that of wild type enzyme
F30V
F30V/I31N
the mutant shows approximately 7fold increase in Km and 8fold decrease in kcat/Km values
H215L
I131N
the mutant shows slightly reduced catalytic efficiency compared to the wild type
I31F
the mutant shows more negative binding energy for hydroxyferuloyl CoA
I31M
the mutant exhibits equal affinity for coumaroyl and hydroxyferulol CoA
I31N
K174M
K174N
the mutant has favorable binding energy for hydroxyferuloyl-CoA
K174R
the mutant has favorable binding energy for hydroxyferuloyl-CoA
L64W
the mutant shows no significant change in Km values compared to the wild type enzyme
R51G
R51G/D77G
the mutant displays 5fold increase in Km and around 9fold reduction in specificity constant
S136A
S212G
S99G
the mutant shows no significant change in Km values compared to the wild type enzyme
V200A
the mutant displays substrate specificity towards coumaroyl-CoA
V200E
V200G
the mutant displays substrate specificity towards coumaroyl-CoA
Y170C
the mutant displays less number of interactions compared to the wild type enzyme
Y170H
A132S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A132T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A43V
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F155H
site-directed mutagenesis, the mutant is only active with feruloyl-CoA as substrate in contrast to the wild-type enzyme
F155Y
site-directed mutagenesis, the mutant exhibits greater catalytic efficiency for sinapoyl-CoA compared to the wild-type PtoCCR7
L192M
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
S123T
the mutant shows reduced activity compared to the wild type enzyme
T154A
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
T154Y
the mutation in SbCCR1 leads to broader substrate specificity and faster turnover. The T154Y mutant exhibits 4.9 and 144fold increases in catalytic efficiency for feruloyl-CoA and 4-coumaroyl-CoA, respectively, over those of wild-type SbCCR1
Y310F
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
additional information
D77G
site-directed mutagenesis, structure comparison to the wild-type enzyme
D77G
the mutant displays equal affinity for caffeoyl-CoA and sinapoyl-CoA
D77G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
F30V
site-directed mutagenesis, structure comparison to the wild-type enzyme
F30V
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
H215L
site-directed mutagenesis, structure comparison to the wild-type enzyme
H215L
the mutant shows no significant change in Km values compared to the wild type enzyme
I31N
site-directed mutagenesis, structure comparison to the wild-type enzyme
I31N
the mutant demonstrates better affinity for sinapoyl CoA over others
K174M
site-directed mutagenesis, structure comparison to the wild-type enzyme
K174M
the mutant shows complete loss of activity with feruloyl-CoA as substrate
R51G
site-directed mutagenesis, structure comparison to the wild-type enzyme
R51G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
R51G
the mutation alters side chain from polar charged to small compact neutral residue, resulting in marked decrease in accessible surface area and leads to loss of interactions with substrate
S136A
site-directed mutagenesis, structure comparison to the wild-type enzyme
S136A
the mutant shows complete loss of activity with feruloyl-CoA as substrate
S212G
site-directed mutagenesis, structure comparison to the wild-type enzyme
S212G
the mutant exhibits the catalytic efficiencies less than 10% of wild type enzyme
S212G
the mutant shows a 2.5fold increase in Km, 7fold reduction in kcat and 15fold decrease in kcat/Km
V200E
site-directed mutagenesis, structure comparison to the wild-type enzyme
V200E
the mutant shows reduced catalytic efficiency compared to the wild type
Y170H
site-directed mutagenesis, structure comparison to the wild-type enzyme
Y170H
the mutant shows complete loss of activity with feruloyl-CoA as substrate
additional information
in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
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two knockout mutants for CCR1. Both have a dwarf phenotype and a delayed senescence. At complete maturity, their inflorescence stems display a 25-35% decreased lignin level, some alterations in lignin structure with a higher frequency of resistant interunit bonds and a higher content in cell wall-bound ferulic esters. Ferulic acid-coniferyl alcohol ether dimers in cell walls show similar levels in wild-type and mutant plants. Expression of CCR2, involved in plant defense, is increased in the mutants and can account for the biosynthesis of lignins in the CCR1-knockout plants. CCR1-mutant plantlets have 3 to 4times less sinapoyl malate than controls and accumulate some feruloyl malate. The same compositional changes occurr in the rosette leaves of greenhouse-grown plants. Relative to the control, stems accumulate unusually high levels of both sinapoyl malate and feruloyl malate as well as more kaempferol glycoside
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
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additional information
Betula platyphylla x Betula pendula
construction of enzyme overexpression and suppression lines, vector transfection using Agrobacterium tumefaciens strain EHA105
additional information
gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR) are fused by means of genetic engineering to generate an artificial bifunctional enzyme. Chimeric 4CL1-CCR is overexpressed in Escherichia coli supplemented with phenylpropanoic acids. Three 4-hydroxycinnamaldehydes, p-coumaraldehyde, caffealdehyde and coniferaldehyde, are thereby biosynthesized and secreted into the culture medium. Extracellular hydroxycinnamoyl-CoA thioesters are not detected, hydroxycinnamoyl-CoA thioesters accumulate only in the cell, because they cannot freely pass through the cellular membrane. The fusion enzyme 4CL1-CCR can catalyze sequential multistep reactions, thereby avoiding the permeability problem of intermediates, which reveals its superiority over a mixture of individual native enzymes. The bifunctional enzyme 4CL1-CCR plays a central role in cellular metabolism by converting phenylpropanoic acids to their corresponding cinnamaldehydes
additional information
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construction of genetically modified poplars, that are downregulated for cinnamoyl-CoA reductase (CCR). 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
additional information
in CCR-deficient poplar, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
