Information on EC 6.2.1.12 - 4-Coumarate-CoA ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
6.2.1.12
-
RECOMMENDED NAME
GeneOntology No.
4-Coumarate-CoA ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
bi uni uni bi ping pong mechanism, catalytic reaction scheme and kinetics, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-coumarate degradation (anaerobic)
-
-
4-hydroxybenzoate biosynthesis I (eukaryotes)
-
-
4-hydroxybenzoate biosynthesis V
-
-
6-gingerol analog biosynthesis
-
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caffeoylglucarate biosynthesis
-
-
coumarins biosynthesis (engineered)
-
-
flavonoid biosynthesis
-
-
naringenin biosynthesis (engineered)
-
-
phaselate biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
suberin monomers biosynthesis
-
-
umbelliferone biosynthesis
-
-
xanthohumol biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
suberin monomers biosynthesis
-
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
-
Phenylalanine metabolism
-
-
Phenylpropanoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
4-Coumarate:CoA ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4-coumarate coenzyme A ligase
-
4-coumarate/coenzyme A ligase
-
-
4-coumarate: CoA ligase
-
4-coumarate: CoA ligase
-
-
4-coumarate: CoA ligase
-
4-coumarate: CoA ligase
Ocimum basilicum CIM SAUMYA
-
-
4-coumarate: CoA ligase
-
4-coumarate: CoA ligase
Ocimum tenuiflorum CIM AYU
-
-
4-coumarate: coenzyme A ligase
-
4-coumarate: coenzyme A ligase
-
4-coumarate: coenzyme A ligase
-
4-coumarate::CoA ligase
-
-
4-coumarate:CoA ligase
-
-
4-coumarate:CoA ligase
-
4-coumarate:CoA ligase
-
-
4-coumarate:CoA ligase
-
4-coumarate:CoA ligase
-
4-coumarate:CoA ligase
Ocimum basilicum CIM SAUMYA
-
-
4-coumarate:CoA ligase
-
4-coumarate:CoA ligase
Ocimum tenuiflorum CIM AYU
-
-
4-coumarate:CoA ligase
-
4-coumarate:CoA ligase
-
-
4-coumarate:CoA ligase
-
4-coumarate:CoA-ligase
-
4-coumarate:CoA-ligase
Ruta graveolens R-20
-
-
4-coumarate:coenzyme A (CoA) ligase
-
-
4-Coumarate:coenzyme A ligase
-
-
-
-
4-Coumarate:coenzyme A ligase
-
-
4-Coumarate:coenzyme A ligase
-
4-Coumarate:coenzyme A ligase
-
4-Coumarate:coenzyme A ligase
-
4-Coumarate:coenzyme A ligase
-
4-Coumarate:coenzyme A ligase
-
-
4-coumarate:coenzyme-A ligase-1
-
-
4-coumaroyl-CoA ligase
-
4-coumaroyl-CoA synthase
-
-
-
-
4-coumaroyl:CoA ligase
-
-
4-Coumaryl-CoA synthetase
-
-
-
-
4CL
-
-
-
-
4CL
Ocimum basilicum CIM SAUMYA
-
-
4CL
Ocimum tenuiflorum CIM AYU
-
-
4CL
Ruta graveolens R-20
-
-
4CL-A1
isozyme
4CL-A1
isozyme
4CL-A1
isozyme
4CL-A1
isozyme
4CL-A2
isozyme
4CL-A2
isozyme
4CL-A2
isozyme
4CL-A2
isozyme
4CL-B
isozyme
4CL-B
isozyme
4CL-B
isozyme
4CL1
Ruta graveolens R-20
isozyme
-
4CL2
Ruta graveolens R-20
isozyme
-
Caffeolyl coenzyme A synthetase
-
-
-
-
caffeoyl-CoA ligase
-
caffeoyl-CoA synthetase
-
caffeoyl-coenzyme A synthetase
-
Clone 4CL14
-
-
-
-
Clone 4CL16
-
-
-
-
coumarate:CoA ligase
-
-
Feruloyl CoA ligase
-
-
-
-
Feruloyl coenzyme A synthetase
-
-
-
-
Hydroxy-cinnamate:CoA ligase
-
-
-
-
Hydroxycinnamate:CoA ligase
-
-
-
-
Hydroxycinnamoyl CoA synthetase
-
-
-
-
OB4CL_ctg4
Ocimum basilicum CIM SAUMYA
-
-
OS4CL
Ocimum tenuiflorum CIM AYU
-
-
p-Coumaroyl CoA ligase
-
-
-
-
p-coumaroyl-CoA ligase
-
-
p-Coumaryl coenzyme A synthetase
-
-
-
-
p-Coumaryl-CoA ligase
-
-
-
-
p-Coumaryl-CoA synthetase
-
-
-
-
p-Hydroxycinnamic acid:CoA ligase
-
-
-
-
p-Hydroxycinnamoyl coenzyme A synthetase
-
-
-
-
Sinapoyl coenzyme A snthetase
-
-
-
-
Synthetase, p-coumaroyl coenzyme A
-
-
-
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type I 4CL
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-
CAS REGISTRY NUMBER
COMMENTARY
37332-51-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
4CL is encoded by a family of four genes 4CL1-4CL4
-
-
Manually annotated by BRENDA team
ecotype Col-0
-
-
Manually annotated by BRENDA team
ecotype Landsberg erecta, genes 4CL1 and 4CL2
-
-
Manually annotated by BRENDA team
isoform 4Cl2, genomic DNA; three isoforms with different substrate specificity and preference, isoforms clustered in class I and II with 4Cl1 and 4Cl2 belonging to class I and 4Cl3 belonging to class II; isoform 4Cl3, genomic DNA; three isoforms with different substrate specificity and preference, isoforms clustered in class I and II with 4Cl1 and 4Cl2 belonging to class I and 4Cl3 belonging to class II
SwissProt
Manually annotated by BRENDA team
isoform 4CL2; isoforms 4CL1, 4CL2 and 4CL3, described experiments performed with isoform 4CL2
SwissProt
Manually annotated by BRENDA team
isoform Cl1, genomic DNA; three isoforms with different substrate specificity and preference, isoforms clustered in class I and II with 4Cl1 and 4Cl2 belonging to class I and 4Cl3 belonging to class II
SwissProt
Manually annotated by BRENDA team
isoforms 4CL1 and 4CL2
-
-
Manually annotated by BRENDA team
fragment; loquat, cultivars LYQ and BS
UniProt
Manually annotated by BRENDA team
Forsythia sp.
-
-
-
Manually annotated by BRENDA team
2 isoenzymes; var. Mandarin
-
-
Manually annotated by BRENDA team
3 isoenzymes
-
-
Manually annotated by BRENDA team
4CL1, cDNA; four isoforms 4CL1-4
SwissProt
Manually annotated by BRENDA team
4CL2, cDNA; four isoforms 4CL1-4
SwissProt
Manually annotated by BRENDA team
4CL3, genomic DNA; four isoforms 4CL1-4
SwissProt
Manually annotated by BRENDA team
4CL4, cDNA; four isoforms 4CL1-4
SwissProt
Manually annotated by BRENDA team
isoforms 4CL1-4CL3
-
-
Manually annotated by BRENDA team
lines ARK8518 and ARK8518R
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
fragment; variant Larix gmelinii japonica
UniProt
Manually annotated by BRENDA team
fragment; variant Larix gmelinii olgensis
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
three isoforms, 4CL2 and 4CL3 belonging to class I and 4CL1 belonging to class II type of 4CL-enzymes
-
-
Manually annotated by BRENDA team
var. chinensis
-
-
Manually annotated by BRENDA team
gene 4CL2; cv. Samsun, gene 4CL2
SwissProt
Manually annotated by BRENDA team
isozyme OB4CL_ctg4
UniProt
Manually annotated by BRENDA team
Ocimum basilicum CIM SAUMYA
isozyme OB4CL_ctg4
UniProt
Manually annotated by BRENDA team
i.e. Ocimum tenuiflorum, isozyme OS4CL
UniProt
Manually annotated by BRENDA team
Ocimum tenuiflorum CIM AYU
i.e. Ocimum tenuiflorum, isozyme OS4CL
UniProt
Manually annotated by BRENDA team
gene R4CL, putative 4-coumarate coenzyme A ligase, i.e. Os02g0177600 protein; gene R4CL
SwissProt
Manually annotated by BRENDA team
Os4Cl1; isozyme Os4Cl1
UniProt
Manually annotated by BRENDA team
Os4Cl1; ssp. japonica, isozyme Os4Cl1
UniProt
Manually annotated by BRENDA team
Os4Cl2; isozyme Os4Cl2
UniProt
Manually annotated by BRENDA team
Os4Cl2; ssp. japonica, isozyme Os4Cl2
UniProt
Manually annotated by BRENDA team
Os4Cl3; isozyme Os4Cl3
SwissProt
Manually annotated by BRENDA team
Os4Cl3; ssp. japonica, isozyme Os4Cl3
SwissProt
Manually annotated by BRENDA team
Os4Cl4; isozyme Os4Cl4
UniProt
Manually annotated by BRENDA team
Os4Cl4; ssp. japonica, isozyme Os4Cl4
UniProt
Manually annotated by BRENDA team
Os4Cl5; isozyme Os4Cl5
UniProt
Manually annotated by BRENDA team
Os4Cl5; ssp. japonica, isozyme Os4Cl5
UniProt
Manually annotated by BRENDA team
isozyme 4CL1; subspecies Physcomitrella patens patens
UniProt
Manually annotated by BRENDA team
isozyme 4CL2; subspecies Physcomitrella patens patens
UniProt
Manually annotated by BRENDA team
isozyme 4CL3; subspecies Physcomitrella patens patens
UniProt
Manually annotated by BRENDA team
isozyme 4CL4; subspecies Physcomitrella patens patens
UniProt
Manually annotated by BRENDA team
isoenzymes not detected
-
-
Manually annotated by BRENDA team
no isoforms detected, one protein with broad substrate specificity
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
Polyporus hispidus
strain UBC 513, light-grown cultures yield preparations with an increased activity
-
-
Manually annotated by BRENDA team
Polyporus hispidus UBC 513
strain UBC 513, light-grown cultures yield preparations with an increased activity
-
-
Manually annotated by BRENDA team
aspen
-
-
Manually annotated by BRENDA team
two isoforms, 4CL1 and 4CL2
-
-
Manually annotated by BRENDA team
hybid poplar, clone H1
-
-
Manually annotated by BRENDA team
3 isoenzymes: I, II, III
-
-
Manually annotated by BRENDA team
isozyme Pl4CL1
UniProt
Manually annotated by BRENDA team
isozyme Pl4CL2
UniProt
Manually annotated by BRENDA team
isozyme 4CL1; strain R-20
UniProt
Manually annotated by BRENDA team
isozyme 4CL2; strain R-20
UniProt
Manually annotated by BRENDA team
Ruta graveolens R-20
isozyme 4CL1; strain R-20
UniProt
Manually annotated by BRENDA team
Ruta graveolens R-20
isozyme 4CL2; strain R-20
UniProt
Manually annotated by BRENDA team
isoforms
-
-
Manually annotated by BRENDA team
isozyme Sa4CL1; isozyme Sa4CL1
UniProt
Manually annotated by BRENDA team
isozyme Sa4CL2; isozyme Sa4CL2
UniProt
Manually annotated by BRENDA team
isozyme Sa4CL3; isozyme Sa4CL3
UniProt
Manually annotated by BRENDA team
cv. Cabernet Sauvignon
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
isozyme Pl4CL1 belongs to the class II 4-coumarate-CoA ligases; isozyme Pl4CL2 belongs to the class I 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; the enzyme belongs to the proteins containing the GEICIRG motif, phylogeny based on AMP-dependent synthetase/ligase domain sequences, overview
evolution
phylogenetically, isozymes Sa4CL1 and Sa4CL2 belong to the class I cluster and Sa4CL3 groups in the class II cluster; phylogenetically, isozymes Sa4CL1 and Sa4CL2 belong to the class I cluster and Sa4CL3 groups in the class II cluster; 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 is a type I 4CL, phylogenetic analysis
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; 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; 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; 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; 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
Ocimum basilicum CIM SAUMYA, Ocimum tenuiflorum CIM AYU
-
the enzyme belongs to the class II 4-coumarate-CoA ligases
-
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
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
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
Ocimum basilicum CIM SAUMYA
-
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
Ocimum tenuiflorum CIM AYU
-
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
-
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; 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
the enzyme is involved in the flavonoid biosynthesis from cinnamic acid, it is the last enzyme of the general phenylpropanoid pathway, overview; the enzyme is involved in the flavonoid biosynthesis from cinnamic acid, it is the last enzyme of the general phenylpropanoid pathway, overview; 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 biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, overview
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis; key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis; key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis; key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis; key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
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
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids; the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids. Isozyme Os4Cl shows potential involvement in flavonoid formation; the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin; the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin; 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
isozyme Pl4CL1 might play a role in isoflavone biosynthesis; isozyme Pl4CL2 might function as a housekeeping enzyme concerning lignification
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; 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; 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
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
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
Os4CL3 may play a role in the synthesis of lignin as well as other phenolic compounds
physiological function
Ocimum tenuiflorum CIM AYU
-
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
-
metabolism
Ocimum tenuiflorum CIM AYU
-
the enzyme is involved in the biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, 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; 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; 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; 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; 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
putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351; putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351
additional information
the enzyme has two conserved putative AMP-binding motifs, the SSGTTGLPKGV and GEICIRG domains
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates; rice 4CL isoforms display different substrate specificities and catalytic turnover rates; rice 4CL isoforms display different substrate specificities and catalytic turnover rates; rice 4CL isoforms display different substrate specificities and catalytic turnover rates; rice 4CL isoforms display different substrate specificities and catalytic turnover rates
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumarate + MgATP2- + tetrapolyphosphate
adenosine 5'-pentaphosphate + ?
show the reaction diagram
-
CoA omitted from the incubation mixture
-
r
4-coumarate + MgATP2- + tripolyphosphate
adenosine 5'-tetraphosphate + ?
show the reaction diagram
-
CoA omitted from the incubation mixture
-
r
AMP + 3-oxo-2-(2'-[Z]-pentenyl)-cyclopentane-1-butanoic acid + CoA
?
show the reaction diagram
-
weak substrate
-
-
?
AMP + 3-oxo-2-(2'-[Z]-pentenyl)-cyclopentane-1-hexanoic acid + CoA
?
show the reaction diagram
-
weak substrate
-
-
?
AMP + dinor-12-oxo-phytodienoic acid + CoA
?
show the reaction diagram
-
-
-
-
?
ATP + (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + CoA
?
show the reaction diagram
-
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
show the reaction diagram
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
84% of the activity relative to ferulate
-
-
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
substrate for 4CL1 but not for 4CL2 and 4CL3
-
?
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
show the reaction diagram
-
high activity
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
ir
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Polyporus hispidus
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Forsythia sp.
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
140% of the activity relative to ferulate
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
94% of the activity relative to ferulate
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
best substrate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
best substrate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
preferred substrate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
high activity
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
high activity
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
100% activity
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism, 4CL2 involved in coenzyme A ester formation and cocatalytic AMP-donor in (di)adenosine polyphosphate synthesis
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
plant phenylpropanoid metabolism, class II enzymes part of flavonoid pathway, class I enzymes probably involved in lignin formation and phenolic compound other than flavonoids
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
isoenzyme 4CL1 exhibits very high activity towards p-coumarate, isoenzymes 4CL2 and 4CL3 are active
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
4-hydroxycinnamic acid, 98%, predominantly trans-isomer
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
highest catalytic efficiency towards 4-coumarate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
assay at pH 7.5
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
52% of the activity with caffeate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Ocimum basilicum CIM SAUMYA
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
best substrate
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Polyporus hispidus UBC 513
-
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Ruta graveolens R-20
100% activity
-
?
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
key enzyme of general phenylpropanoid metabolism
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme of B-ring-deoxy flavonoid biosymthesis
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
physiological role in lignin biosynthesis
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
the isoenzymes can play an important role in the control of the monomeric composition of lignins
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme has an important role in the determination of the composition and the amount of lignin in tobacco plants
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
key enzyme of phenylpropanoid metabolism
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
4-coumarate-CoA ligase is the last enzyme of the general phenylpropanoid metabolism, supplying substrates for lignin formation and other individual phenylpropanoid pathways
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme is involved in the resistance response of soybean against pathogen attack. The different substrate affinities for substituted cinnamic acids and the differential regulation of the 3 isoenzymes, may play a pivotal role in distributing substituted cinnamate intermediates at a branch point of general phenylpropanoid metabolism into subsequent specific pathways
-
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
68% of the activity relative to ferulate
-
-
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
12% of the activity relative to 4-coumarate
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
17% of the activity relative to ferulate
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
41% of the activity relative to p-hydroxycinnamate
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
isoenzyme I is active, no activity is detectable with isoenzyme II and III
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
18% of the activity relative to ferulate
-
-
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
show the reaction diagram
-
isoenzyme 4CL2, weak activity, isoenzyme 4CL1 and 4CL3 show no activity
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Polyporus hispidus
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
61% of the activity relative to p-hydroxycinnamate
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
at 4% of the activity relative to 4-coumarate
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
48% of the activity relative to ferulate
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
14% of the activity relative to 4-coumarate
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
86% of the activity relative to ferulate
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
isoenzyme III is active, no activity is detectable with isoenzyme I and II
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
low activity
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
low activity
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
high activity
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
same activity as with 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
-
isoenzyme 4CL1, 4CL2 and 4CL3 show activity
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
48% activity compared to 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
86% activity compared to 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
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
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Polyporus hispidus UBC 513
-
-
-
-
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Ruta graveolens R-20
86% activity compared to 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Ruta graveolens R-20
48% activity compared to 4-coumarate
-
?
ATP + caffeic acid + CoA
AMP + diphosphate + 4-caffeoyl-CoA
show the reaction diagram
-
3,4-dihydroxycinnamic acid, 98%, 3,4-dihydroxycinnamic acid, 98%, predominantly trans-isomer
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
ir
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
ir
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
14% of the activity relative to ferulate
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
10% of the activity relative to 4-coumarate
-
-
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
low activity
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
roughly 30% of activity
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
same Vmax like 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
5.0% activity compared to 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
54% activity compared to 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
9% of the activity with caffeate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
Ruta graveolens R-20
54% activity compared to 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
Ruta graveolens R-20
5.0% activity compared to 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + 4-cinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + cinnamic acid + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
3-phenyl-2-propenoic acid, 98%
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
show the reaction diagram
-
weak substrate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Polyporus hispidus
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Forsythia sp.
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
67% of the activity relative to p-hydroxycinnamate
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
49% of the activity relative to 4-coumarate
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
3% of the activity relative to 4-coumarate
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
high activity
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
M293P/K320L mutant enzyme, no substrate for wild type enzyme
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
only 4CL1 and 4CL3, no substrate for 4CL2, some 4CL2 mutants are active with ferulate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
only 4CL1, no substrate for 4CL2
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
only 4CL1, no substrate for 4CL2
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
roughly 60% of activity
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
same activity as with 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
substrate for 4CL1 and 4CL2, very poor substrate for 4CL3
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
very poor substrate for the wild type enzyme, effective substrate for M293P/K320L mutant enzyme
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
isoenzyme 4CL2 and 4CL3 are active, no activity with isoenzyme 4CL1
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
2.5% activity compared to 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
50.5% activity compared to 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
strong preference for ferulate by isozyme Os4CL2, high activity
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
16% of the activity with caffeate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Polyporus hispidus UBC 513
-
-
-
-
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Ruta graveolens R-20
2.5% activity compared to 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Ruta graveolens R-20
50.5% activity compared to 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
show the reaction diagram
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
show the reaction diagram
-
-
?
ATP + ferulic acid + CoA
AMP + diphosphate + 4-feruloyl-CoA
show the reaction diagram
-
4-hydroxy-3-methoxycinnamic acid, 99%
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
show the reaction diagram
-
weak substrate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + indole propanoic acid + CoA
?
show the reaction diagram
-
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
show the reaction diagram
-
-
-
-
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
show the reaction diagram
-
as effective as ferulate
-
-
ATP + nonanoate + CoA
AMP + diphosphate + nonanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
show the reaction diagram
-
weak substrate
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
show the reaction diagram
-
weak substrate
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
-
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
substrate for 4CL1 but not for 4CL2 and 4CL3
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
isoenzymes 4CL2 and 4CL3 are active, isoenzyme 4CL1 is inactive
-
?
ATP + sinapic acid + CoA
AMP + diphosphate + 4-sinapoyl-CoA
show the reaction diagram
-
3,5-dimethoxy-4-hydroxycinnamic acid, 98%, predominantly trans isomer
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
48% of the activity relative to ferulate
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
isoenzyme I is active, no activity with isoenzyme II and III
-
-
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
isoenzyme 1 is active with sinapoate, isoenzyme 2 not
-
-
ATP + tetradecanoate + CoA
AMP + diphosphate + tetradecanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
-
-
?
CTP + ferulate + CoA
CMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
7.7% of the activity relative to ATP
-
-
GTP + ferulate + CoA
GMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
5.7% of the activity relative to ATP
-
-
ITP + ferulate + CoA
IMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
20.2% of the activity relative to ATP
-
-
UTP + ferulate + CoA
UMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
12.5% of the activity relative to GTP
-
-
MgATP2-
diadenosine 5',5'',P1,P4-tetraphosphate + ?
show the reaction diagram
-
no additional substrate, CoA omitted from the incubation mixture
-
?
additional information
?
-
-
absolute requirement for ATP
-
-
-
additional information
?
-
-
the enzyme from different tissues varies significantly in substrate specificity
-
-
-
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
-
additional information
?
-
-
in ATP-diphosphate exchange reaction absolute specificity for cinnamate
-
-
-
additional information
?
-
-
ATP-diphosphate exchange reaction is activated by cinnamate, dihydro-4-coumarate, caprylate and malonate
-
-
-
additional information
?
-
-
inactive against sinapic acid
-
-
?
additional information
?
-
inactive against sinapic acid
-
-
?
additional information
?
-
inactive against sinapic acid and ferulic acid
-
-
?
additional information
?
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
-
?
additional information
?
-
-
the isoform 4CL1 has a strong substrate preference for p-coumarate, but lacked the activity for ferulate and sinapate. The other hand, 4CL2 and 4CL3 display activity towards sinapate and also possess high activity towards caffeate as well as p-coumarate
-
-
-
additional information
?
-
-
biosynthesis of lignin monomers occurs via the phenylpropanoid pathway, in which the enzyme 4-coumarate-CoA ligase plays a key role by catalyzing the formation of hydroxycinnamoyl-CoA esters, subsequently reduced to the corresponding monolignols hydroxycinnamoyl alcohols, overview, cis-regulatory elements involved in the developmental and wound-induced regulation of the 4CL gene family members, stress-regulated expression, overview
-
-
-
additional information
?
-
-
the 4-coumarate-CoA ligase, 4CL, gene family members are involved in channeling carbon flow into branch pathways of phenylpropanoid metabolism, identification of regulatory genes, overview
-
-
-
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
?
-
-
three key enzymes: phenylalanine ammonia-lyase, cinnamate-4-hydroxylase, and 4-coumarate-coenzyme A ligase, catalyzing the biosynthesis of these compounds during berry development, contents of gallic, protocatechuic, gentisic and caffeic acid all change drastically during berry development, while other compounds containing 4-hydroxybenzoic, vanillic, syringic, chlorogenic, 4-coumaric, ferulic and sinapic acid vary only slightly
-
-
-
additional information
?
-
-
the enzyme performs synthesis of (5,7-dihydroxy-4-chromanone)-propenoic acid in concert with chalcone synthase, chalcone isomerase, and flavanone 3-hydroxylase, fed with a number of aromatic acrylic acids, mechanism, overview
-
-
-
additional information
?
-
4CL has a key role in the biosynthesis of monolignols in softwood species
-
-
-
additional information
?
-
-
a 7fold increase in 4CL activity is observed in elicited cultures after 24 h of chitosan treatment (200 mg/l) as compared to control
-
-
-
additional information
?
-
sinapate is not accepted as a substrate
-
-
-
additional information
?
-
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
-
additional information
?
-
isozyme Pl4CL2 has a broader substrate specificity than Pl4CL1
-
-
-
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
?
-
no activity with benzoate and 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, ferulate and caffeate
-
-
-
additional information
?
-
no activity with sinapic acid
-
-
-
additional information
?
-
no activity with either sinapate or 4-hydroxybenzoate. The more hydroxyl groups are present, the better is the activity of the enzyme. Methoxy groups on the aromatic ring have a negative effect on enzyme activity. It is possible that methoxy groups cause a steric obstruction. No activity can be measured if there is no acryl group present in the substrate
-
-
-
additional information
?
-
Ocimum tenuiflorum CIM AYU
no activity with sinapic acid
-
-
-
additional information
?
-
Ruta graveolens R-20
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
L7Z3F8
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Q6ETN3
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
T1NXG6
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
S4WX39
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
U3MJP5, U3MNX0
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
D5LLN7, D5LNB5, D5LNB6
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
P31687, Q8S564, Q8S5C1, Q8S5C2
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Q9S725
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
plant phenylpropanoid metabolism, 4CL2 involved in coenzyme A ester formation and cocatalytic AMP-donor in (di)adenosine polyphosphate synthesis
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Q42524, Q9S725
plant phenylpropanoid metabolism, class II enzymes part of flavonoid pathway, class I enzymes probably involved in lignin formation and phenolic compound other than flavonoids
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
the enzyme is involved in the phenylpropanoid pathway
-
?
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
key enzyme of general phenylpropanoid metabolism
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme of B-ring-deoxy flavonoid biosymthesis
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
physiological role in lignin biosynthesis
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
the isoenzymes can play an important role in the control of the monomeric composition of lignins
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme has an important role in the determination of the composition and the amount of lignin in tobacco plants
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
key enzyme of phenylpropanoid metabolism
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
4-coumarate-CoA ligase is the last enzyme of the general phenylpropanoid metabolism, supplying substrates for lignin formation and other individual phenylpropanoid pathways
-
-
-
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
enzyme is involved in the resistance response of soybean against pathogen attack. The different substrate affinities for substituted cinnamic acids and the differential regulation of the 3 isoenzymes, may play a pivotal role in distributing substituted cinnamate intermediates at a branch point of general phenylpropanoid metabolism into subsequent specific pathways
-
-
-
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Ocimum basilicum CIM SAUMYA
S4WX39
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
T1NXG6
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
T1NXG6
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
U3MJP5, U3MNX0
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
F1CYZ6
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
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
T1NXG6
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + 4-cinnamoyl-CoA
show the reaction diagram
D5LLN7, D5LNB5, D5LNB6
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
L7Z3F8
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
T1NXG6
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
U3MJP5, U3MNX0
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
show the reaction diagram
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
Ocimum tenuiflorum CIM AYU
T1NXG6
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
T1NXG6
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
U3MJP5, U3MNX0
-
-
?
additional information
?
-
-
biosynthesis of lignin monomers occurs via the phenylpropanoid pathway, in which the enzyme 4-coumarate-CoA ligase plays a key role by catalyzing the formation of hydroxycinnamoyl-CoA esters, subsequently reduced to the corresponding monolignols hydroxycinnamoyl alcohols, overview, cis-regulatory elements involved in the developmental and wound-induced regulation of the 4CL gene family members, stress-regulated expression, overview
-
-
-
additional information
?
-
-
the 4-coumarate-CoA ligase, 4CL, gene family members are involved in channeling carbon flow into branch pathways of phenylpropanoid metabolism, identification of regulatory genes, overview
-
-
-
additional information
?
-
Q6ETN3
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
?
-
-
three key enzymes: phenylalanine ammonia-lyase, cinnamate-4-hydroxylase, and 4-coumarate-coenzyme A ligase, catalyzing the biosynthesis of these compounds during berry development, contents of gallic, protocatechuic, gentisic and caffeic acid all change drastically during berry development, while other compounds containing 4-hydroxybenzoic, vanillic, syringic, chlorogenic, 4-coumaric, ferulic and sinapic acid vary only slightly
-
-
-
additional information
?
-
B8QN50
4CL has a key role in the biosynthesis of monolignols in softwood species
-
-
-
additional information
?
-
-
a 7fold increase in 4CL activity is observed in elicited cultures after 24 h of chitosan treatment (200 mg/l) as compared to control
-
-
-
additional information
?
-
U3MJP5, U3MNX0
isozyme Pl4CL2 has a broader substrate specificity than Pl4CL1
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
33% of the activation compared to Mg2+
Ca2+
can substitute Mg2+; can substitute Mg2+; can substitute Mg2+
Co2+
-
divalent cation required, Mg2+, Mn2+ and Co2+ are equally effective
Co2+
-
97% of the activation relative to Mg2+
Co2+
-
can partially substitute for Mg2+
K+
strictly K+-dependent. Half-maximal activity is obtained at 6 mM K+
Mg2+
Forsythia sp.
-
-
Mg2+
-
required in a molar ratio of 1:1 with ATP
Mg2+
-
divalent cation required, Mg2+, Mn2+ and Co2+ are equally effective
Mg2+
-
required in a molar ratio of 1:1 with ATP
Mg2+
-
required
Mg2+
-
optimal concentration 10 mM; required
Mg2+
-
required
Mg2+
required; required
Mg2+
required; required; required
Mg2+
-
required
Mg2+
required; required; required; required; required
Mn2+
-
divalent cation required, Mg2+, Mn2+ and Co2+ are equally effective
Mn2+
-
97% of the activation compared to Mg2+
Mn2+
-
85% of the activation relative to Mg2+
Mn2+
-
can partially substitute for Mg2+
Ni2+
-
81% of the activation relative to Mg2+
Ni2+
-
can partially substitute for Mg2+
Zn2+
-
can partially substitute for Mg2+, very low activity
Mn2+
can substitute Mg2+; can substitute Mg2+; can substitute Mg2+
additional information
-
no effect with Ca2+
additional information
strict dependence of Sa4CLs on a divalent cation, no activity with Cu2+; strict dependence of Sa4CLs on a divalent cation, no activity with Cu2+; strict dependence of Sa4CLs on a divalent cation, no activity with Cu2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-methylenedioxycinnamic acid
-
potent inhibitor
4-chloromercuribenzoate
-
-
4-coumarate
-
above 0.1 mM
4-coumarate
-
-
4-coumarate
-
inhibition above 0.6 mM
4-coumarate
-
strong competitive inhibitor for the other substrates
alachlor
-
slight inhibition
bentazone
-
slight inhibition
butachlor
-
-
caffeate
-
inhibition above 0.2 mM
caffeate
-
strong competitive inhibitor for the other substrates
chlornitrofen
-
-
CoA
-
substrate inhibition
CoASH
-
above 0.1 mM
coniferin
-
-
dimepiperate
-
-
fenoxaprop-ethyl
-
-
ferulate
-
strong substrate inhibition above 0.2 mM
ferulate
-
inhibition above 0.4 mM
ferulate
-
strong competitive inhibitor for the other substrates
Heat-labile high-molecular-weight factor from tobacco stem extract
-
-
-
iodoacetamide
-
-
Ionic strength
-
activity of isoenzyme 1 decreases steadily with increasing ionic strength at least in the range from 0.1 to 0.8 M Tris-HCl, highest rate of isoenzyme 2 activity is obtained at concentrations of about 0.3 M Tris-HCl
-
linuron
-
slight inhibition
mefenacet
-
slight inhibition
Naringenin
-
-
Naringenin
-
the wild-type enzyme is strongly allosterically inhibited by naringenin, a downstream product of the pathway. The feedback inhibition is probably exerted through a unique allosteric domain, docking-based model and in silico modeling for the interaction of naringenin with the wild-type enzyme. Mutations Q274H and F269L, but not V186G, lead to loss of feedback inhibition by naringenin
nitrofen
-
slight inhibition
Pentachlorophenol
-
slight inhibition
pretilachlor
-
slight inhibition
propanil
-
72% inhibition at 0.1 mM
propanil
-
a herbicide, 71.8% inhibition at 0.1 mM, uncompetitive inhibition towards 4-coumaric acid
pyrazosulfuron-ethyl
-
slight inhibition
simazine
-
slight inhibition
simetryn
-
slight inhibition
swep
-
98% inhibition at 0.1 mM
swep
-
a herbicide, 97.1% inhibition at 0.1 mM, uncompetitive inhibition towards 4-coumaric acid
thenylchlor
-
-
thiobencarb
-
slight inhibition
molinate
-
slight inhibition
additional information
-
the sinapate-converting activity is not inhibited by other cinnamate derivatives, such as p-coumarate, caffeate or ferulate
-
additional information
-
development and optimization of a high-throughput miniaturized screening system of plant growth inhibitors targeting 4CL in the phenylpropanoid pathway, in vitro inhibitor screening using 28 existing herbicides, overview, no inhibition by pendimethalin, trifluralin, alloxydim-sodium, bispyribac-sodium, dimethenamid, metolachlor, pyrazolate, bensulfuron-methyl, and imazosulfuron
-
additional information
-
in vitro inhibitor screening using existing herbicides, screening assay optimization, overview
-
additional information
95% suppression of 4CL can lead to an about 50% reduction in lignin content and affects lignin composition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
-
treatment of fruits
additional information
-
developmental and wound-induced regulation, stress-regulated expression
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
2-coumarate
-
isoenzyme 2
0.18
2-coumarate
-
isoenzyme 1
0.23
3,4,5-trimethoxycinnamate
-
isoenzyme 1
0.049
3,4-dimethoxycinnamate
-
4CL1
0.083
3,4-dimethoxycinnamate
-
0.55
3,4-dimethoxycinnamate
-
-
0.028
3-coumarate
-
-
0.03
3-coumarate
-
isoenzyme 2
0.00166
4-coumarate
pH 7.5, 30C
0.0025
4-coumarate
pH 7.5, 22C
0.0031
4-coumarate
isozyme 4CL2, at pH 7.8 and 32C
0.0035
4-coumarate
pH 7.8, 22C
0.0036
4-coumarate
-
4CL2, pH 7.5, 30C
0.0036
4-coumarate
-
recombinant F269L/K415T, pH 7.8, 30C
0.0039
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.004
4-coumarate
recombinant isozyme 4CL1
0.0049
4-coumarate
-
recombinant V186I/V187L, pH 7.8, 30C
0.0049
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.0051
4-coumarate
-
recombinant V186G, pH 7.8, 30C
0.0055
4-coumarate
isozyme 4CL1, pH 7.8, 32C
0.0062
4-coumarate
-
-
0.0073
4-coumarate
pH 7.5, 22C
0.00747
4-coumarate
-
recombinant wild-type enzyme, pH 7.8, 30C
0.009
4-coumarate
-
0.009
4-coumarate
-
4CL3
0.009
4-coumarate
pH 7.5, 22C
0.0091
4-coumarate
pH 7.8, 22C
0.01
4-coumarate
-
isoenzyme II
0.01
4-coumarate
-
0.0103
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0104
4-coumarate
-
recombinant F239S, pH 7.8, 30C
0.0119
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.013
4-coumarate
-
isoenzyme III
0.016
4-coumarate
recombinant isozyme 4CL2
0.0168
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.017
4-coumarate
-
isoenzyme 2
0.017
4-coumarate
-
5-hydroxyferulate
0.0179
4-coumarate
-
recombinant Q274H, pH 7.8, 30C
0.022
4-coumarate
-
0.022
4-coumarate
-
M293P/K320L mutant enzyme
0.023
4-coumarate
room temperature
0.025
4-coumarate
-
4CL1, pH 7.8, room temperature
0.027
4-coumarate
-
M293P/K320L mutant enzyme, pH 7.0, 30C
0.029
4-coumarate
recombinant isozyme 4CL3
0.031
4-coumarate
-
-
0.032
4-coumarate
-
isoenzyme 1
0.032
4-coumarate
-
ATP
0.038
4-coumarate
room temperature
0.042
4-coumarate
-
isoenzyme I
0.042
4-coumarate
-
0.042
4-coumarate
-
4CL2
0.05
4-coumarate
-
4CL1
0.056
4-coumarate
-
4CL1, pH 7.5, 30C
0.08
4-coumarate
-
room temperature
0.103
4-coumarate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.136
4-coumarate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.143
4-coumarate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.212
4-coumarate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.22
4-coumarate
-
4CL2, pH 7.8, room temperature
0.233
4-coumarate
-
wild-type enzyme, pH 7.0, 30C
0.233
4-coumarate
-
wild-type enzyme
0.252
4-coumarate
room temperature
0.282
4-coumarate
pH not specified in the publication, 30C, isozyme Os4Cl3
0.246
4-coumaric acid
-
-
0.38
4-methoxycinnamate
-
isoenzyme 1
0.5
4-methoxyferulate
-
-
0.012
5-hydroxyferulate
-
isoenzyme 1
0.12
5-hydroxyferulate
-
isoenzyme 2
0.34
5-hydroxyferulate
-
-
0.064
adenosine 5'-tetraphosphate
-
reverse reaction, M293P/K320L mutant enzyme, pH 7.0, 30C
0.004
ATP
-
wild-type enzyme, pH 7.0, 30C
0.013
ATP
30C, pH 7.0
0.029
ATP
-
K457S mutant enzyme
0.036
ATP
-
-
0.065
ATP
-
isoenzyme 2
0.151
ATP
-
K211S mutant enzyme
0.163
ATP
-
wild type
0.17
ATP
-
3-coumarate, , isoenzyme 1
0.173
ATP
-
C403 mutant enzyme
0.24
ATP
-
E401Q mutant enzyme
1.507
ATP
-
R449Q mutant enzyme
0.0009
caffeate
pH 7.5, 22C
0.00494
caffeate
pH 7.5, 30C
0.005
caffeate
-
K457S mutant enzyme
0.0058
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0068
caffeate
pH 7.5, 22C
0.0109
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.011
caffeate
room temperature
0.0125
caffeate
pH 7.5, 22C
0.013
caffeate
-
4CL2
0.014
caffeate
-
isoenzyme 2
0.014
caffeate
-
2-coumarate
0.014
caffeate
-
K211S mutant enzyme
0.0149
caffeate
pH 7.8, 22C
0.0161
caffeate
-
-
0.018
caffeate
-
C403A mutant enzyme
0.02
caffeate
room temperature
0.022
caffeate
-
wild-type enzyme
0.024
caffeate
-
wild type
0.024
caffeate
wild type enzyme
0.024
caffeate
-
wild-type enzyme, pH 7.0, 30C
0.025
caffeate
recombinant isozyme 4CL1
0.025
caffeate
30C, pH 7.0
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
0.028
caffeate
-
E401Q mutant enzyme
0.0293
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.035
caffeate
-
4CL1, pH 7.5, 30C
0.037
caffeate
isozyme 4CL2, at pH 7.8 and 32C
0.04
caffeate
-
isoenzyme 1
0.041
caffeate
-
M293P/K320L mutant enzyme
0.042
caffeate
-
4CL2, pH 7.5, 30C
0.045
caffeate
recombinant isozyme 4CL2
0.048
caffeate
-
M293P/K320L mutant enzyme, pH 7.0, 30C
0.0484
caffeate
isozyme 4CL1, pH 7.8, 32C
0.05
caffeate
-
4CL3
0.081
caffeate
-
4CL1
0.154
caffeate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.234
caffeate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.262
caffeate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.282
caffeate
pH not specified in the publication, 30C, isozyme Os4Cl3
0.374
caffeate
room temperature
0.4
caffeate
-
R449Q mutant enzyme
0.725
caffeate
recombinant isozyme 4CL3
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
0.021
cinnamate
pH 7.5, 22C
0.0217
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.023
cinnamate
pH 7.5, 22C
0.0282
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.033
cinnamate
pH 7.5, 22C
0.037
cinnamate
isozyme 4CL2, at pH 7.8 and 32C
0.05
cinnamate
recombinant isozyme 4CL1
0.0544
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.059
cinnamate
isozyme 4CL1, pH 7.8, 32C
0.064
cinnamate
recombinant isozyme 4CL3
0.066
cinnamate
recombinant isozyme 4CL2
0.28
cinnamate
-
-
0.292
cinnamate
-
M293P/K320L mutant enzyme, pH 7.0, 30C
1.048
cinnamate
-
room temperature
1.1
cinnamate
-
4CL3
1.3
cinnamate
-
isoenzyme 1
1.7
cinnamate
-
4CL2
2.07
cinnamate
room temperature
4.4
cinnamate
-
4CL1
4.5
cinnamate
-
isoenzyme 2
6.32
cinnamate
room temperature
6.35
cinnamate
-
wild-type enzyme, pH 7.0, 30C
6.63
cinnamate
room temperature
0.0032
CoA
-
-
0.5
CoA
30C, pH 7.0
0.004
CoASH
-
isoenzyme 2
0.007
CoASH
-
isoenzyme 1
0.0009
ferulate
pH 7.5, 22C
0.0021
ferulate
-
-
0.0022
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.00302
ferulate
pH 7.5, 30C
0.0035
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.004
ferulate
-
4CL1
0.0046
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0047
ferulate
-
-
0.0054
ferulate
pH 7.5, 22C
0.00609
ferulate
-
recombinant wild-type enzyme, pH 7.8, 30C
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
0.009
ferulate
-
isoenzyme 1
0.0106
ferulate
-
recombinant F269L/K415T, pH 7.8, 30C
0.011
ferulate
-
isoenzyme II
0.0119
ferulate
-
recombinant F239S, pH 7.8, 30C
0.0137
ferulate
-
-
0.0142
ferulate
-
recombinant V186G, pH 7.8, 30C
0.015
ferulate
-
isoenzyme III
0.02
ferulate
-
-
0.02
ferulate
-
caffeate
0.02
ferulate
-
ferulate, , isoenzyme I
0.03
ferulate
-
M293P/K320L mutant enzyme
0.033
ferulate
-
-
0.0353
ferulate
-
recombinant Q274H, pH 7.8, 30C
0.046
ferulate
-
-
0.046
ferulate
-
M293P/K320L mutant enzyme, pH 7.0, 30C
0.05
ferulate
pH 7.5, 22C
0.057
ferulate
-
4CL1, pH 7.8, room temperature
0.073
ferulate
recombinant isozyme 4CL2
0.079
ferulate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.0884
ferulate
pH 7.8, 22C
0.102
ferulate
-
room temperature
0.112
ferulate
-
4CL1, pH 7.5, 30C
0.13
ferulate
-
isoenzyme 2
0.139
ferulate
-
4CL2, pH 7.5, 30C
0.14
ferulate
-
4CL2
0.166
ferulate
room temperature
0.18
ferulate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.187
ferulate
recombinant isozyme 4CL1
0.199
ferulate
room temperature
0.309
ferulate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.38
ferulate
pH not specified in the publication, 30C, isozyme Os4Cl3
0.384
ferulate
pH not specified in the publication, 30C, isozyme Os4Cl1
0.8
ferulate
recombinant isozyme 4CL3
3.1
ferulate
-
4CL3
0.026
isoferulate
-
-
0.1
isoferulate
-
3,4-dimethoxycinnamate, , isoenzyme 1
0.15
isoferulate
-
isoenzyme 2
0.69
p-methoxycinnamate
-
-
0.005
sinapate
-
4CL1
0.0589
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.001
sinapoate
-
-
0.011
sinapoate
-
isoenzyme 1
0.022
sinapoate
-
isoenzyme I
0.02576
trans-cinnamate
pH 7.5, 30C
0.141
trans-cinnamate
pH 7.8, 22C
0.664
trans-cinnamate
pH 7.8, 22C
0.336
m-methoxycinnamate
-
-
additional information
additional information
Km values for all mutant enzymes given
-
additional information
additional information
-
kinetics in presence of inhibitors
-
additional information
additional information
kinetic analysis of the recombinant engineered isozyme At4CL1-VvSTS fusion enzyme, overview
-
additional information
additional information
steady-state MichaelisMenten kinetics; steady-state MichaelisMenten kinetics; steady-state MichaelisMenten kinetics
-
additional information
additional information
-
catalytic reaction scheme and kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0082
4-coumarate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0395
4-coumarate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.047
4-coumarate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.048
4-coumarate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.285
4-coumarate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.49
4-coumarate
Solanum lycopersicum
-
recombinant V186I/V187L, pH 7.8, 30C
0.58
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.66
4-coumarate
Solanum lycopersicum
-
recombinant wild-type enzyme, pH 7.8, 30C
0.7 - 1
4-coumarate
Ocimum tenuiflorum
T1NXG6
pH 7.5, 30C
0.742
4-coumarate
Solanum lycopersicum
-
recombinant F269L/K415T, pH 7.8, 30C
0.96
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1.02
4-coumarate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1.28
4-coumarate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1.623
4-coumarate
Solanum lycopersicum
-
recombinant V186G, pH 7.8, 30C
1.819
4-coumarate
Solanum lycopersicum
-
recombinant F239S, pH 7.8, 30C
4.05
4-coumarate
Solanum lycopersicum
-
recombinant Q274H, pH 7.8, 30C
0.0087
caffeate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.014
caffeate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.036
caffeate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0445
caffeate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.255
caffeate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.36
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.44
caffeate
Ocimum tenuiflorum
T1NXG6
pH 7.5, 30C
0.78
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.8
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.92
caffeate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
0.0061
cinnamate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.017
cinnamate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0188
cinnamate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0213
cinnamate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.182
cinnamate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.26
cinnamate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.3
cinnamate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.37
cinnamate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
5.5
CoA
Acetobacterium woodii
F1CYZ6
30C, pH 7.0
0.0068
ferulate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.032
ferulate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.034
ferulate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0385
ferulate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.299
ferulate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.34
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.38
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.49
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
0.569
ferulate
Solanum lycopersicum
-
recombinant V186G, pH 7.8, 30C
0.57
ferulate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
0.636
ferulate
Solanum lycopersicum
-
recombinant F269L/K415T, pH 7.8, 30C
1.063
ferulate
Solanum lycopersicum
-
recombinant wild-type enzyme, pH 7.8, 30C
1.107
ferulate
Solanum lycopersicum
-
recombinant F239S, pH 7.8, 30C
1.56
ferulate
Ocimum tenuiflorum
T1NXG6
pH 7.5, 30C
0.053
sinapate
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.47
trans-cinnamate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
0.58
trans-cinnamate
Ocimum tenuiflorum
T1NXG6
pH 7.5, 30C
0.97
trans-cinnamate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
2.04
ferulate
Solanum lycopersicum
-
recombinant Q274H, pH 7.8, 30C
additional information
additional information
Oryza sativa
P17814, Q42982, Q67W82, Q6ETN3, Q6ZAC1
isozyme Os4CL1 displays a very low turnover rate
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18.23
4-coumarate
Solanum lycopersicum
-
recombinant V186G, pH 7.8, 30C
1215
88.4
4-coumarate
Solanum lycopersicum
-
recombinant wild-type enzyme, pH 7.8, 30C
1215
100
4-coumarate
Solanum lycopersicum
-
recombinant V186I/V187L, pH 7.8, 30C
1215
112
4-coumarate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1215
120
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1215
130
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1215
174.6
4-coumarate
Solanum lycopersicum
-
recombinant F239S, pH 7.8, 30C
1215
206.1
4-coumarate
Solanum lycopersicum
-
recombinant F269L/K415T, pH 7.8, 30C
1215
226.3
4-coumarate
Solanum lycopersicum
-
recombinant Q274H, pH 7.8, 30C
1215
230
4-coumarate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1215
364
4-coumarate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1215
60
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1276
62
caffeate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1276
120
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1276
410
caffeate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1276
10
cinnamate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C; pH 7.5, 22C; pH 7.5, 22C
1823
6.5
ferulate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1047
10
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1047
40.16
ferulate
Solanum lycopersicum
-
recombinant V186G, pH 7.8, 30C
1047
57.79
ferulate
Solanum lycopersicum
-
recombinant Q274H, pH 7.8, 30C
1047
60.06
ferulate
Solanum lycopersicum
-
recombinant F269L/K415T, pH 7.8, 30C
1047
90
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1047
92.87
ferulate
Solanum lycopersicum
-
recombinant F239S, pH 7.8, 30C
1047
174.5
ferulate
Solanum lycopersicum
-
recombinant wild-type enzyme, pH 7.8, 30C
1047
360
ferulate
Sorbus aucuparia
D5LLN7, D5LNB5, D5LNB6
pH 7.5, 22C
1047
1.46
trans-cinnamate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1544
3.3
trans-cinnamate
Pueraria montana var. lobata
U3MJP5, U3MNX0
pH 7.8, 22C
1544
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
caffeate
-
4CL1 with 4-coumarate as substrate, pH 7.5, 30C
0.012
caffeate
-
4CL2 with 4-coumarate as substrate, pH 7.5, 30C
0.1
ferulate
-
4CL1 with 4-coumarate as substrate, pH 7.5, 30C
0.3
ferulate
-
4CL2 with 4-coumarate as substrate, pH 7.5, 30C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0396
propanil
Nicotiana tabacum
-
-
0.006
swep
Nicotiana tabacum
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.013
-
purified leaf enzyme, room temperature
0.13
-
purified cell culture enzyme, room temperature
0.33
-
purified xylem enzyme, room temperature
0.34
-
K211S mutant enzyme with caffeate as substrate
0.37
-
R449Q mutant enzyme with caffeate as substrate
0.46
-
K457S mutant enzyme with caffeate as substrate
2.64
-
E401Q mutant enzyme with caffeate as substrate
3.624
-
purified recombinnat enzyme, substrate 4-coumaric acid
5.64
-
C403A mutant enzyme with caffeate as substrate
12.5
-
wild type with caffeate as substrate
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Polyporus hispidus
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
changes in phenolic acids contents in fruits during development, overview
additional information
-
38.3 U/mg protein, 1 unit is defined as the amount of enzyme causing an increase in absorbtion, day 2 of storage at 1C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
adenosine 5' tetraphosphate formation
7
-
ATP-diphosphate exchange reaction
7 - 8
-
ATP-diphosphate exchange
7.2 - 7.6
-
-
7.3
-
formation of feruloyl-CoA
7.5
-
-
7.5
-
assay at
7.5
assay at; assay at
7.5
assay at; assay at; assay at; assay at; assay at
7.5 - 8
Polyporus hispidus
-
-
7.6 - 8
-
Tris-HCl or sodium-potassium phosphate buffer
7.7
-
formation of 4-coumaroyl-CoA, isoenzyme 2
7.8
-
assay at
7.8
-
assay at
7.8 - 8
-
formation of 4-coumaroyl-CoA
8.3
-
formation of 4-coumaroyl-CoA, isoenzyme 1
8.5
-
-
8.9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
-
half maximal activity, adenosine 5' tetraphosphate foormation
6.2 - 8
-
half-maximum activity at pH 6.2 and 8
6.8 - 7.5
-
6.8: about 80% of maximal activity, 7.5: maximal activity
7 - 8.5
Polyporus hispidus
-
the activity is greatly reduced below pH 7.0 and above pH 8.5
7.2 - 9.5
-
about 55% of maximal activity at pH 7.2 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
assay at room temperature; assay at room temperature
22
assay at room temperature
22 - 30
assay at
30
-
-
30
-
assay at
30
assay at; assay at; assay at; assay at; assay at
40
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20C: about 70% of maximal activity, 40C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
sequence calculation; sequence calculation
5.6
sequence calculation
5.8
calculated from amino acid sequence, isozyme 4CL1
6.58
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isozyme Os4CL2 is specifically expressed in the anther
Manually annotated by BRENDA team
-
apparent ectopic GUS expression in the cotyledons and mature leaves outside of the vascular tissues in some cases, but this was restricted to the veins in the wounded area in a pattern reminiscent of 4CL3 expression, overview
Manually annotated by BRENDA team
; isozyme 4CL1 is mostly expressed in the flower
Manually annotated by BRENDA team
mature, low expression level
Manually annotated by BRENDA team
in the lemma, palea, stamens, and pistil
Manually annotated by BRENDA team
Ruta graveolens R-20
-
; isozyme 4CL1 is mostly expressed in the flower
-
Manually annotated by BRENDA team
-
the enzyme is located predominantly in the secondarily thickened walls and the parenchyma cells of mesocarp vascular tissue, developmental changes in enzyme activity, overview
Manually annotated by BRENDA team
expression of 4CL in cultivar BS fruit increases during the first 6 days, again slightly preceding a rise in enzyme activity, while expression in ripening cultivar LYQ fruit remains at a relatively low level
Manually annotated by BRENDA team
-
infected with a non pathogenic isolate of Botrytis cinerea
Manually annotated by BRENDA team
-
apparent ectopic GUS expression in the cotyledons and mature leaves outside of the vascular tissues in some cases, but this was restricted to the veins in the wounded area in a pattern reminiscent of 4CL3 expression, overview
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
in developing vascular bundle cells as well as in parenchyma cells
Manually annotated by BRENDA team
Ocimum basilicum CIM SAUMYA, Ocimum tenuiflorum CIM AYU
-
-
-
Manually annotated by BRENDA team
-
3 isoenzymes are present at very low level of activity, isoenzyme II is the major isoenzyme
Manually annotated by BRENDA team
-
enzyme activity dominates in mesophyll protoplasts and in vascular elements, the enzyme from different tissues varies significantly in substrate specificity
Manually annotated by BRENDA team
negligible expression in the root; negligible expression in the root
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
exodermis and epidermis cells
Manually annotated by BRENDA team
Ocimum basilicum CIM SAUMYA, Ocimum tenuiflorum CIM AYU
-
-
-
Manually annotated by BRENDA team
Ruta graveolens R-20
-
negligible expression in the root; negligible expression in the root
-
Manually annotated by BRENDA team
-
only isoenzyme I is detectable
Manually annotated by BRENDA team
-
etiolated
Manually annotated by BRENDA team
; isozyme 4CL2 is expressed mostly in the shoot
Manually annotated by BRENDA team
Ruta graveolens R-20
-
; isozyme 4CL2 is expressed mostly in the shoot
-
Manually annotated by BRENDA team
Forsythia sp.
-
-
Manually annotated by BRENDA team
-
young, lignifying
Manually annotated by BRENDA team
-
activity is controlled by light
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
in epidermis cells and sheath parenchyma cells, in which no lignin is being synthesized
Manually annotated by BRENDA team
Ocimum basilicum CIM SAUMYA, Ocimum tenuiflorum CIM AYU
-
-
-
Manually annotated by BRENDA team
glandular trichome-rich tissue
Manually annotated by BRENDA team
glandular trichome-rich tissue
Manually annotated by BRENDA team
Ocimum basilicum CIM SAUMYA, Ocimum tenuiflorum CIM AYU
-
glandular trichome-rich tissue
-
Manually annotated by BRENDA team
-
differentiating
Manually annotated by BRENDA team
-
3 isoenzymes present
Manually annotated by BRENDA team
-
4CL2 is the major isoform in developing xylem extract, 4CL3 is a very minor one
Manually annotated by BRENDA team
Ruta graveolens R-20
-
;
-
Manually annotated by BRENDA team
additional information
-
developmental and wound-induced regulation
Manually annotated by BRENDA team
additional information
no N-terminal extension of Pl4CL2; Pl4CL1 has an N-terminal extension of twenty-one amino acid residues
Manually annotated by BRENDA team
additional information
quantitative reverse transcription-PCR expression analysis at different developmental stages, 2, 4 and 6 weeks after seed germination, overview
Manually annotated by BRENDA team
additional information
differential expression in all tissues during the developmental stages, transcript expression patterns, quantitative real-time PCR analysis, overview
Manually annotated by BRENDA team
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; quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview; quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview; quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview; quantitative reverse transcription-PCR expression analysis of isozymes during growth and development, overview
Manually annotated by BRENDA team
additional information
Ocimum tenuiflorum CIM AYU
-
quantitative reverse transcription-PCR expression analysis at different developmental stages, 2, 4 and 6 weeks after seed germination, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isozyme Sa4CL3 contains a 49-amino acid N-terminal extension, which includes a chloroplast sorting signal
Manually annotated by BRENDA team
additional information
-
subcellular enzyme localization in berries
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
-
gel filtration
616
41000
-
gel filtration
615
50000
-
gel filtration
595
55000
-
gel filtration
606
55000
-
gel filtration
607
57000
-
gel filtration
614
57000
-
gel filtration
620
60000
-
SDS-PAGE
653496
62380
calculated from amino acid sequence, isozyme 4CL1
694698
64000
-
-
605
64000
SDS-PAGE, isozyme 4CL3
694601
65000
SDS-PAGE, isozyme 4CL1; SDS-PAGE, isozyme 4CL2
694601
66000
SDS-PAGE
653477
67000
-
gel filtration
611
75000
-
also 2 small peaks with MW 20000 are detected, 2 isoenzymes, which differ in ionic properties and substrate specificity can exist in two or three molecular weight forms. There is evidence that theses forms are under certain circumstances interconcertible, gel filtration
612
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 62000, SDS-PAGE
?
x * 86000, recombinant enzyme, SDS-PAGE
?
x * 65000, isozyme 4CL1, SDS-PAGE
?
x * 62384, calculated from amino acid sequence, isozyme 4CL1
?
x * 59500, about, isozyme Sa4CL1, sequence calculation; x * 60100, about, isozyme Sa4CL2, sequence calculation; x * 66200, about, isozyme Sa4CL3, sequence calculation
?
x * 62480, recombinant N-terminally His6-tagged enzyme, SDS-PAGE
?
x * 59560, sequence calculation
?
x * 60000, SDS-PAGE
?
Ocimum tenuiflorum CIM AYU
-
x * 62480, recombinant N-terminally His6-tagged enzyme, SDS-PAGE
-
?
Ruta graveolens R-20
-
x * 62384, calculated from amino acid sequence, isozyme 4CL1
-
monomer
-
1 * 63000, SDS-PAGE
additional information
-
homology modeling
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant isozyme At4CL1 and engineered isozyme At4CL1-VvSTS fusion enzyme, X-ray diffraction structure determination and analysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
stable
607
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
-
rapid inactivation
607
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete stabilization in presence of 30% glycerol or 30% ethylene glycol
-
sucrose stabilizes
-
purified enzyme is very labile, no stabilizer found
-
30% glycerol or 15% ethylene glycol stabilizes
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethylene glycol
-
30% ethylene glycol stabilizes. Loss of activity after 7 days is reduced from 80% to about 25%
Glycerol
-
30% glycerol stabilizes. Loss of activity after 7 days is reduced from 80% to about 25%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10% or 30% glycerol, or 10% ethylene glycol, stable for 10 days
-
-20C, 50% glycerol
-
1C, after two days decrease in enzyme activity
-
-20C, several weeks without significant loss of activity
-
crude enzyme preparation is unstable in buffered aqueous solution at temperatures at or above 0C
-
complete loss of activity in crude enzyme extract after 4 days at 4-6C. 0.92 M sucrose can reduce the loss of activity to 20%. Complete stabilization in presence of 30% glycerol or 30% ethylene glycol
-
-20C, 10 mM sodium/potassium phosphate, pH 7.0, 42 mM mercaptoethanol, 20% ethyleneglycol, stable for several months
-
-20C, stable for 2 or 3 months, crude enzyme extract
-
stable for several weeks at -20C or two days at 0C, in 0.1 M Tris-HCl buffer, pH 7.5, 30% glycerol or 15% ethylene glycol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant enzyme using His-tag
-
using His-tag
-
partial
-
recombinant protein using His-tag
-
recombinant enzyme 6.3fold from Escherichia coli strain JM105 by a multistep process involving anion exchange chromatography and gel filtration
-
recombinant enzyme from Escherichia coli strain JM105 by a multistep process involving anion exchange chromatography and gel filtration
-
recombinant enzyme from Escherichia coli strain BL21 to near homogeneity
recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag; recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag; recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag; recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag; recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag
Ni-NTA column chromatography; Ni-NTA column chromatography; Ni-NTA column chromatography; Ni-NTA column chromatography
recombinant protein using His-tag
-
partial
Polyporus hispidus
-
recombinant protein using His-tag
-
native and recombinant enzymes
-
Sephadex G-25 gel filtration; Sephadex G-25 gel filtration
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
DNA and amino acid sequence determination and analysis, sequence comparisons
; expression in together with tyramine N-hydroxycinnamoyltransferase in Escherichia coli
-
cloning of 4CL, encoded by a family of four genes 4CL1-4CL4
-
expressed in Escherichia coli as His-tag fusion protein and in native form
expressed in Escherichia coli M15 as His-tag fusion protein
-
expressed in Escherichia coli M15[pRP4] as His-tag fusion protein
-
expressed in Escherichia coli strains DH5alpha and M15
-
expression in Escherichia coli M15(pRP4)
expression in Lactococcus lactis
-
expression of isozyme At4CL1, and of the engineered fusion protein of Arabidopsis thaliana At4CL1 and Vitis vinifera stilbene synthase, VvSTS
insertion of phenylalanine ammonia lyase from the red yeast Rhodosporidium toruloides, 4-coumarate:coenzyme A ligase from the plant Arabidopsis thaliana, and chalcone synthase from the plant Hypericum androsaemum into a yeast expression vector. Each gene is under the control of its own galactose-inducible promoter. Yeast harboring this vector produces naringenin and pinocembrin through the phenylpropanoid pathway, as well as four by-products, two of which are identified as phloretin and 2',4',6'-trihydroxydihydrochalcone through a sequential side reaction
nucleotide sequence of cDNA
-
transgenic Arabidopsis plants containing the At4CL1 or At4CL2 promoter fused to the beta-glucuronidase reporter gene show developmentally regulated GUS expression in the xylem tissues of the root and shoot, identification of regulatory genes involved in the developmental regulation of At4CL, overview
-
expressed in Escherichia coli as His-tag fusion protein
expression in Escherichia coli as His-tag fusion protein
-
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, quantitative real-time PCR expression analysis
expressed in Escherichia coli strains JM109 and BLR(DE3)
-
DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis; DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
expression in Saccharomyces cerevisiae and Escherichia coli strain BL21, co-expression with stilbene synthase, gene STS, from Vitis vinifera establishing an resveratrol expression system with 4-coumaric acid as precursor, biosynthetic pathway of resveratrol, overview
gene 4CL, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM105
-
DNA and amino acid sequence determination and analysis, sequence comparisons
DNA and amino acid sequence determination and analysis, sequence comparisons, transient expression of OS4CL-GFP-fusion protein in Arabidopsis thaliana protoplast cytosol, expression of N-terminally His6-tagged OS4CL in Escherichia coli
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 Os4CL3, 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
gene R4CL, expression in Escherichia coli strain BL21
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 Os4Cl3, 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
two distinct 4CL genes, highly homologous for several hundred base pairs
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
60-66% sequence identity with 4-coumarate:CoA ligase sequences from herbaceous angiosperms
-
expressed in Escherichia coli as His-tag fusion protein
-
a binary vector containing Pto4CL1p promoter fused with 4CL1 gene is transferred into tobacco. The activity of the 4CL1 enzyme doubles in the stems of transgenic tobacco but does not increase in the leaves. The content of lignin is increased 25% in the stem but there is no increase in the leaves of transgenic tobacco
-
expressed in Escherichia coli as His-tag fusion protein
-
expressed in Sf9 cells using the baculovirus system
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)/pET28a, subcloning in Escherichia coli strain M15; DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)/pQE30, subcloning in Escherichia coli strain M15
expressed in Saccharomyces cerevisiae; expressed in Saccharomyces cerevisiae
expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of wild-type and mutants in Saccharomyces cerevisiae expressing also the CHS gene
-
expression of GST-tagged isozyme Sa4CL1 in Escherichia coli; expression of His6-tagged isozyme Sa4CL2 in Escherichia coli; expression of His6-tagged isozyme Sa4CL3 in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CarE and CarD (and thus the caffeate reduction operon) are induced in cells grown in the presence of cinnamate, sinapate, caffeate, ferulate, or 4-coumarate
exposure of tea shoots to 50-100 microM catechins leads to down-regulation of the expression of 4CL
strong positive correlation coefficient between catechins content and the expression of Cs4Cl throughout a variety of environmental conditions such as drought stress, abscisic acid and gibberellic acid treatments, and wounding. Tea clones with high levels of catechins have higher expression of 4CL whereas tea clones with lower catechins exhibit lower expression of this gene
the enzyme expression is reduced by abscisic acid treatment. The Hc4CL gene is downregulated at early time points and then upregulated 24 h after H2O2 treatment, after which the transcript level returns to a negative level relative to the control. The enzyme also shows biphasic expression in response to wounding. Specifically, the transcript is highly expressed at 6 h and then decreases sharply at 12 h with a second induction at 24 h
Hc4CL is upregulated by NaCl treatment, reaching its maximum level at 24 h after treatment. The enzyme is induced by cold and drought treatment. The Hc4CL gene is downregulated at early time points and then upregulated 24 h after H2O2 treatment, after which the transcript level returns to a negative level relative to the control. The enzyme also shows biphasic expression in response to wounding. Specifically, the transcript is highly expressed at 6 h and then decreases sharply at 12 h with a second induction at 24 h
isozyme Os4CL1 is downregulated by UV radiation when dark-adapted rice plants are illuminated with UV-containing white light; isozyme Os4CL3 is downregulated by UV radiation when dark-adapted rice plants are illuminated with UV-containing white light; isozyme Os4CL4 is downregulated by UV radiation when dark-adapted rice plants are illuminated with UV-containing white light; isozyme Os4CL5 is downregulated by UV radiation when dark-adapted rice plants are illuminated with UV-containing white light
Os4CL2 is strongly activated by UV irradiation, the isozyme is induced by up to 16fold at 12 h after the onset of irradiation, and expression remains high at 24 h after treatment
expression of Pl4CL2 is not significantly influenced in methyl jasmonate-treated samples
expression of Pl4CL1 is increased more than 3fold in the 24 h methyl jasmonate-treated samples
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C403A
-
activity reduced to 45% of wild-type level, no effect on Km values for ATP and caffeate
E401Q
-
activity reduced to 21% of wild-type level, no effect on Km values for ATP and caffeate
K211S
-
activity reduced to 2.7% of wild-type level
K320A
new substrate specificity, accepts ferulate as substrate
K320L
new substrate specificity, accepts ferulate as substrate
K445T
-
activity reduced to 0.2% of wild-type level
K457S
-
activity reduced to 4% of wild-type level
K540N
-
no activity
L356A
-
only little effect on activity
M293A
new substrate specificity, accepts ferulate as substrate
M293A/V294L
substitution of valine decreases Km for ferulate 2-3fold compared to single methionine substitution mutant
M293F
no reaction with ferulate, increases Km for caffeate
M293P
new substrate specificity, accepts ferulate as substrate
M293P/K320L
-
strongly affects Km for all substrates, capable in using ferulate, capable in adenosine 5'-tetraphosphate formation at 10fold higher rate than wild type enzyme
M293P/K320L
-
effectively uses ferulate as substrate, changes in Km for all substrates
M293P/V294M
substitution of valine decreases Km for ferulate 2-3fold compared to single methionine substitution mutant
M293W
no reaction with ferulate
N256A/M293P/K320L
-
effectively uses ferulate and cinnamate as substrates, 10fold reduced activity with caffeate
R449Q
-
activity reduced to 3% of wild-type level, Km values significantly increased
V294L
slightly reduced activity with caffeate, no activity with ferulate
V294M
slightly reduced activity with caffeate, no activity with ferulate
V355A
-
strongly reduced activity
V355A/L356A
-
strongly reduced activity
E340A
-
4CL1-mutant, activity almost completely abolished
G333A
-
4CL1-mutant, activity almost completely abolished
G337A
-
4CL1-mutant, activity almost completely abolished
G342A
-
4CL1-mutant, activity almost completely abolished
I346A
-
4CL1-mutant, very low activity with all substrates
L344A
-
4CL1-mutant, activity almost completely abolished
M338A
-
4CL1-mutant, activity almost completely abolished
P285A
-
4CL1-mutant, very low activity with all substrates
P286A
-
4CL1-mutant, minor changes in activity
P343A
-
4CL1-mutant, very low activity with all substrates
Q334A
-
4CL1-mutant, very low activity with all substrates
T331A
-
4CL1-mutant, minor changes in activity
T339A
-
4CL1-mutant, activity almost completely abolished
V284A
-
4CL1-mutant, minor changes in activity
F239A
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239N
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239R
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239S
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme. The mutant strain produces more naringenin chalcone compared to the wild-type
F269G
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
F269I
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
F269L
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type, loss of feedback inhibition by naringenin
F269L/K415T
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme
Q274D
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type; site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
Q274E
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
Q274G
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
Q274H
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme, loss of feedback inhibition by naringenin, the mutant strain produces more naringenin chalcone compared to the wild-type
Q274S
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
V186A
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
V186G
-
site-directed mutagenesis, the mutant shows highly increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme. The mutant strain produces highly increased naringenin chalcone content compared to the wild-type
V186I
-
site-directed mutagenesis, the mutant strain produces highly increased naringenin chalcone content compared to the wild-type
V186I/V187L
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid compared to the wild-type enzyme, but no activity with ferulic acid
V186L
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
V235M/A325G
-
site-directed mutagenesis, highly unstable inactive mutant
M293Y
no reaction with ferulate, increases Km for caffeate
additional information
-
construction of chimeric proteins consisting of fragments of isoforms 4CL1 and 4CL2
additional information
-
domain exchange experiments with gramicidine synthetase from Bacillus brevis
additional information
-
generation of ethyl methyl sulfate mutagenized populations of At4CL1-GUS and At4CL2-GUS transgenic lines, DNA methylation of the proximal promoter sequences of the transgene only in the mutant lines, while silencing in the seedlings of the At4CL1-GUS lines is root-specific in seedlings, it affects all organs in the At4CL2-GUS lines, analysis of endogenous 4CL expression in epimutant lines, and phenotype analysis, overview
additional information
-
expression of artificial zinc finger chimeras, e.g. transgenic lines expressing chimeras with the KOX/KRAB repression domain or the VP16 activation domain, regulates the enzyme in positive and negative manner, repression of gene 4CL1 results in reduced lignin production and severely diminished lignin distribution, while enzyme upregulation causes an increase in lignin content and ectopic lignin distribution by plant stems
additional information
the engineered fusion protein of Arabidopsis thaliana At4CL1 and Vitis vinifera stilbene synthase VvSTS shows 15fold increased resveratrol levels relative to yeast expressing the individual enzymes, but only less than 3fold increased 4-coumaroyl-CoA ligase or stilbene synthase activities compared to the wild-type enzymes. Co-localization of the two enzyme active sites within 70 A of each other provides the basis for enhanced in vivo synthesis of resveratrol
M348A
-
4CL1-mutant, activity almost completely abolished
additional information
-
construction of hybrid enzymes using different portions of isoforms 4CL1-4CL3, some of the constructed proteins were found to be inactive
Y336A
-
4CL1-mutant, activity almost completely abolished
additional information
transient silencing of the OS4CL gene in planta by RNA interference
additional information
Ocimum tenuiflorum CIM AYU
-
transient silencing of the OS4CL gene in planta by RNA interference
-
F269V
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
additional information
-
interactions of the Q274H mutation with other mutants, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
heterologous expression of biosynthetic genes encoding 4-coumarate:coenzyme A ligase and tyramine N-hydroxycinnamoyltransferase cloned from Arabidopsis thaliana and pepper, respectively. Simultaneous supplementation of substrates to the recombinant Escherichia coli results in the secretion of multiple tyramine derivatives into the medium at high yield: 4-coumaroyltyramine at 189 mg/l, feruloyltyramine at 135 mg/l, caffeoyltyramine at 40 mg/l. The recombinant Escherichia coli also produces, albeit at low concentration, a range of dopamine derivatives such as feruloyldopamine
drug development
-
the enzyme is a target for developing effective plant growth inhibitors, overview
synthesis
-
crude aspen CoA ligase can be effectively and economically used to synthesize caffeoyl CoA
biotechnology
-
viability of a flavonoid network to utilize acrylic acid analogues and describe the combinatorial mutasynthesis of novel unnatural flavonoids using recombinant Saccharomyces cerevisiae, overview
synthesis
-
viability of a flavonoid network to utilize acrylic acid analogues and describe the combinatorial mutasynthesis of novel unnatural flavonoids using recombinant Saccharomyces cerevisiae, overview