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Information on EC 6.2.1.12 - 4-coumarate-CoA ligase and Organism(s) Oryza sativa and UniProt Accession P17814

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.12 4-coumarate-CoA ligase
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This record set is specific for:
Oryza sativa
UNIPROT: P17814 not found.
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The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
4-coumarate:coa ligase, 4-coumarate:coenzyme a ligase, 4-coumarate-coa ligase, 4-coumarate coa ligase, 4-coumarate coenzyme a ligase, at4cl1, 4-coumaroyl-coa ligase, os4cl, pl4cl1, pl4cl2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-Coumarate:coenzyme A ligase
-
4-coumarate coenzyme A ligase
-
4-Coumarate:coenzyme A ligase
4-coumaroyl-CoA synthase
-
-
-
-
4-Coumaryl-CoA synthetase
-
-
-
-
Caffeolyl coenzyme A synthetase
-
-
-
-
Clone 4CL14
-
-
-
-
Clone 4CL16
-
-
-
-
Feruloyl CoA ligase
-
-
-
-
Feruloyl coenzyme A synthetase
-
-
-
-
Hydroxy-cinnamate:CoA ligase
-
-
-
-
Hydroxycinnamate:CoA ligase
-
-
-
-
Hydroxycinnamoyl CoA synthetase
-
-
-
-
p-Coumaroyl CoA ligase
-
-
-
-
p-Coumaryl coenzyme A synthetase
-
-
-
-
p-Coumaryl-CoA ligase
-
-
-
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p-Coumaryl-CoA synthetase
-
-
-
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p-Hydroxycinnamic acid:CoA ligase
-
-
-
-
p-Hydroxycinnamoyl coenzyme A synthetase
-
-
-
-
Sinapoyl coenzyme A snthetase
-
-
-
-
Synthetase, p-coumaroyl coenzyme A
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-coumarate:CoA ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37332-51-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
show the reaction diagram
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
show the reaction diagram
low activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
show the reaction diagram
-
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0119 - 0.136
4-coumarate
0.0293 - 0.234
caffeate
0.0094
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0083 - 0.079
ferulate
0.0039 - 0.282
4-coumarate
0.0058 - 0.282
caffeate
0.0157 - 0.0544
cinnamate
0.0022 - 0.384
ferulate
0.0589
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0087
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0061
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0068
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0395 - 0.285
4-coumarate
0.014 - 0.255
caffeate
0.017 - 0.182
cinnamate
0.032 - 0.299
ferulate
0.053
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isozyme Os4CL2 is specifically expressed in the anther
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
in rice, Os4CL2 belongs to the same clade as type II 4CLs in dicots, while the rest of the 4CLs (Os4CL1/3/4/5) belongs to a separate cluster, named type III, which is distinct from the lignin-associated type I 4CLs found in dicots
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
physiological function
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
evolution
in rice, Os4CL2 belongs to the same clade as type II 4CLs in dicots, while the rest of the 4CLs (Os4CL1/3/4/5) belongs to a separate cluster, named type III, which is distinct from the lignin-associated type I 4CLs found in dicots
malfunction
suppression of Os4CL3 expression results in significant lignin reduction, shorter plant growth, and other morphological changes. 4CL-suppressed transgenics also display decreased panicle fertility, which may be attributed to abnormal anther development as a result of disrupted lignin synthesis, isozyme Os4Cl3 suppressed phenotype, overview
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86000
x * 86000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 86000, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography and removal of the GST-tag
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Os4CL1, DNA and amino acid sequence determination and analysis, gene structure and phylogenetic analysis
isozyme Os4Cl1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21
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 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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, Y.; Jeon, Y.; Lee, J.S.; Kim, B.; Lee, C.H.; Ahn, J.
Enzymatic synthesis of phenolic CoAs using 4-coumarate:coenzyme A ligase (4CL) from rice
Bull. Korean Chem. Soc.
28
365-366
2007
Oryza sativa (Q6ETN3)
-
Manually annotated by BRENDA team
Sun, H.; Li, Y.; Feng, S.; Zou, W.; Guo, K.; Fan, C.; Si, S.; Peng, L.
Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice
Biochem. Biophys. Res. Commun.
430
1151-1156
2013
Oryza sativa (P17814), Oryza sativa (Q42982), Oryza sativa (Q67W82), Oryza sativa (Q6ETN3), Oryza sativa (Q6ZAC1), Oryza sativa
Manually annotated by BRENDA team
Gui, J.; Shen, J.; Li, L.
Functional characterization of evolutionarily divergent 4-coumarate:coenzyme a ligases in rice
Plant Physiol.
157
574-586
2011
Oryza sativa (P17814), Oryza sativa (Q42982), Oryza sativa (Q67W82), Oryza sativa (Q6ETN3), Oryza sativa (Q6ZAC1), Oryza sativa
Manually annotated by BRENDA team