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ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
low activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
?
additional information
?
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
best substrate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
low activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
high activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
best substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
high activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
low activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
low activity
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
low activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
high activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
strong preference for ferulate by isozyme Os4CL2, high activity
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of 4-coumaric acid into coumaroyl-CoA and a few related substrates into their corresponding products such as cinnamoyl-CoA, caffeoyl-CoA, and feruloyl-CoA in a process utilizing ATP, and thus channels the common, phenylalanine-derived building block into the widely distinct branches of general phenylpropanoid metabolism
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
-
no activity with sinapate and caffeate
-
-
?
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0.0049 - 0.282
4-coumarate
0.0282
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.0039 - 0.212
4-coumarate
0.0094 - 0.0544
cinnamate
0.0589
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0049
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.282
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.0109
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.282
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.0035
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.38
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.0039
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0103
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0119
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0168
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.103
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.136
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.143
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.212
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.0058
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0261
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0276
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0293
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.154
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.234
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.262
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.0094
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0157
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0217
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0544
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0022
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0046
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0069
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0083
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.079
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.18
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.309
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.384
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
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0.285
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.255
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.182
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.299
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.0082 - 0.048
4-coumarate
0.0061 - 0.0213
cinnamate
0.053
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
additional information
additional information
-
0.0082
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0395
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.047
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.048
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0087
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.014
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.036
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0445
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0061
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.017
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0188
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0213
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0068
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.032
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.034
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0385
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
additional information
additional information
isozyme Os4CL1 displays a very low turnover rate
-
additional information
additional information
isozyme Os4CL1 displays a very low turnover rate
-
additional information
additional information
isozyme Os4CL1 displays a very low turnover rate
-
additional information
additional information
isozyme Os4CL1 displays a very low turnover rate
-
additional information
additional information
isozyme Os4CL1 displays a very low turnover rate
-
additional information
additional information
-
isozyme Os4CL1 displays a very low turnover rate
-
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in the lemma, palea, stamens, and pistil
brenda
in developing vascular bundle cells as well as in parenchyma cells
brenda
exodermis and epidermis cells
brenda
-
brenda
in epidermis cells and sheath parenchyma cells, in which no lignin is being synthesized
brenda
isozyme Os4CL2 is specifically expressed in the anther
brenda
-
brenda
-
brenda
-
brenda
-
brenda
additional information
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
-
Os4CL3 is expressed in thickening vascular cells and non-thickening parenchyma cells throughout rice growth, immunohistochemic in situ analysis, quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
additional information
-
quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
brenda
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evolution
in rice, Os4CL2 belongs to the same clade as type II 4CLs in dicots, while the rest of the 4CLs (Os4CL1/3/4/5) belongs to a separate cluster, named type III, which is distinct from the lignin-associated type I 4CLs found in dicots
malfunction
suppression of Os4CL3 expression results in significant lignin reduction, shorter plant growth, and other morphological changes. 4CL-suppressed transgenics also display decreased panicle fertility, which may be attributed to abnormal anther development as a result of disrupted lignin synthesis, isozyme Os4Cl3 suppressed phenotype, overview
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
evolution
in rice, Os4CL2 belongs to the same clade as type II 4CLs in dicots, while the rest of the 4CLs (Os4CL1/3/4/5) belongs to a separate cluster, named type III, which is distinct from the lignin-associated type I 4CLs found in dicots
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
physiological function
Os4CL3 may play a role in the synthesis of lignin as well as other phenolic compounds
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids. Isozyme Os4Cl shows potential involvement in flavonoid formation
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin, 4-coumaric acid and ferulic acid are the two main substrates of the enzyme for monolignol biosynthesis in rice
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
-
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
-
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
-
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
-
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
-
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
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gene Os4CL3, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
gene R4CL, expression in Escherichia coli strain BL21
isozyme Os4Cl3, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
gene Os4CL1, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
gene Os4CL2, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
gene Os4CL4, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
gene Os4CL5, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
isozyme Os4Cl1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
isozyme Os4Cl2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
isozyme Os4Cl4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
isozyme Os4Cl5, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
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Lee, Y.; Jeon, Y.; Lee, J.S.; Kim, B.; Lee, C.H.; Ahn, J.
Enzymatic synthesis of phenolic CoAs using 4-coumarate:coenzyme A ligase (4CL) from rice
Bull. Korean Chem. Soc.
28
365-366
2007
Oryza sativa (Q6ETN3)
-
brenda
Sun, H.; Li, Y.; Feng, S.; Zou, W.; Guo, K.; Fan, C.; Si, S.; Peng, L.
Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice
Biochem. Biophys. Res. Commun.
430
1151-1156
2013
Oryza sativa (P17814), Oryza sativa (Q42982), Oryza sativa (Q67W82), Oryza sativa (Q6ETN3), Oryza sativa (Q6ZAC1), Oryza sativa
brenda
Gui, J.; Shen, J.; Li, L.
Functional characterization of evolutionarily divergent 4-coumarate:coenzyme a ligases in rice
Plant Physiol.
157
574-586
2011
Oryza sativa (P17814), Oryza sativa (Q42982), Oryza sativa (Q67W82), Oryza sativa (Q6ETN3), Oryza sativa (Q6ZAC1), Oryza sativa
brenda