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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
evolution
isozyme Pl4CL1 belongs to the class II 4-coumarate-CoA ligases
evolution
isozyme Pl4CL2 belongs to the class I 4-coumarate-CoA ligases
evolution
phylogenetically, isozymes Sa4CL1 and Sa4CL2 belong to the class I cluster and Sa4CL3 groups in the class II cluster
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the proteins containing the GEICIRG motif, phylogeny based on AMP-dependent synthetase/ligase domain sequences, overview
evolution
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the enzyme is a type I 4CL, phylogenetic analysis
evolution
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the enzyme belongs to the class II 4-coumarate-CoA ligases
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evolution
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the enzyme belongs to the class II 4-coumarate-CoA ligases
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malfunction
a significant reduction in the expression levels is observed for OB4CL_ctg4-related transcripts in suppressed trichome compared with transcripts similar to the other four isoforms, OB4CL_ctg1, 2, 3 and 5
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
malfunction
transient RNAi suppression of OS4CL in leaves causes a reduction in leaf eugenol content and trichome transcript level, with a considerable increase in endogenous 4-coumaric, ferulic, trans-cinnamic and caffeic acids, but no significant effect of OS4CL suppression on the total lignin content
malfunction
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growth reduction is observed when the enzyme gene expression is inhibited by more than 70%
malfunction
loss of isoform 4CL1 leads to reduction in lignin content but no growth defect
malfunction
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a significant reduction in the expression levels is observed for OB4CL_ctg4-related transcripts in suppressed trichome compared with transcripts similar to the other four isoforms, OB4CL_ctg1, 2, 3 and 5
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malfunction
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transient RNAi suppression of OS4CL in leaves causes a reduction in leaf eugenol content and trichome transcript level, with a considerable increase in endogenous 4-coumaric, ferulic, trans-cinnamic and caffeic acids, but no significant effect of OS4CL suppression on the total lignin content
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metabolism
4-coumarate:CoA ligases are a group of essential enzymes involved in the phenylpropanoid-derived compound pathway, which converts hydroxylated cinnamic acids into their corresponding thioesters. The PDC pathway as well as its branch pathways generates various classes of secondary compounds, including lignin, flavones, flavonols, anthocyanins, isoflavonoids, and furanocoumarins
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
metabolism
the enzyme is involved in the biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, overview
metabolism
the enzyme is involved in the flavonoid biosynthesis from cinnamic acid, it is the last enzyme of the general phenylpropanoid pathway, overview
metabolism
the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion
metabolism
isoform 4CL3 plays an important role in flavonoid biosynthesis
metabolism
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the enzyme is involved in the biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, overview
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physiological function
isozyme Pl4CL1 might play a role in isoflavone biosynthesis
physiological function
isozyme Pl4CL2 might function as a housekeeping enzyme concerning lignification
physiological function
metabolite channeling of intermediates towards eugenol by a specific 4-coumarate:CoA ligase and involvement of the enzyme in creation of virtual compartments through substrate utilization and committing metabolites for eugenol biosynthesis at an early stage of the pathway, overview
physiological function
Os4CL3 may play a role in the synthesis of lignin as well as other phenolic compounds
physiological function
Sorbus aucuparia cell cultures accumulate biphenyl and dibenzofuran phytoalexins from the starter substrate benzoyl-CoA in response to elicitor treatment involving cinnamate:CoA ligase and benzoate:CoA ligase, but not 4-coumarate:CoA ligase
physiological function
the enzyme is a key regulatory enzyme of the phenylpropanoid pathway that regulates the activation of cinnamic acid, leading to the synthesis of flavonoids and 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
physiological function
isoform 4CL1 is required for wild type levels of lignin biosynthesis
physiological function
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metabolite channeling of intermediates towards eugenol by a specific 4-coumarate:CoA ligase and involvement of the enzyme in creation of virtual compartments through substrate utilization and committing metabolites for eugenol biosynthesis at an early stage of the pathway, overview
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additional information
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putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351
additional information
putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351
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
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rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
the enzyme has two conserved putative AMP-binding motifs, the SSGTTGLPKGV and GEICIRG domains
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
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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
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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