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Information on EC 6.2.1.12 - 4-coumarate-CoA ligase and Organism(s) Petroselinum crispum and UniProt Accession P14913

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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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Petroselinum crispum
UNIPROT: P14913 not found.
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The taxonomic range for the selected organisms is: Petroselinum crispum
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-coumaroyl-CoA synthase
-
-
-
-
4-Coumaryl-CoA synthetase
-
-
-
-
4CL
-
-
-
-
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
-
-
-
-
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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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-coumarate:CoA ligase (AMP-forming)
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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 + 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
-
no activity
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 4-coumarate + CoA
?
show the reaction diagram
-
key enzyme of general phenylpropanoid metabolism
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 4-methoxyferulate + CoA
AMP + diphosphate + 4-methoxyferuloyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-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 + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
show the reaction diagram
-
no activity
-
-
?
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
?
show the reaction diagram
-
key enzyme of general phenylpropanoid metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
33% of the activation compared to Mg2+
Mg2+
-
required in a molar ratio of 1:1 with ATP
Mn2+
-
97% of the activation compared to Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
-
4-coumarate
-
-
iodoacetamide
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
3,4-dimethoxycinnamate
-
-
0.028
3-coumarate
-
-
0.5
4-methoxyferulate
-
-
0.34
5-hydroxyferulate
-
-
0.014
caffeate
-
2-coumarate
0.28
cinnamate
-
-
0.02 - 0.033
ferulate
0.026
isoferulate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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ATP-diphosphate exchange
7.8 - 8
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formation of 4-coumaroyl-CoA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
4CL2_PETCR
544
0
59783
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
-
gel filtration
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete stabilization in presence of 30% glycerol or 30% ethylene glycol
-
sucrose stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity in crude enzyme extract after 4 days at 4-6°C. 0.92 M sucrose can reduce the loss of activity to 20%. Complete stabilization in presence of 30% glycerol or 30% ethylene glycol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
two distinct 4CL genes, highly homologous for several hundred base pairs
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
a de novo pathway for the production of raspberry ketone is assembled using four heterologous genes, encoding phenylalanine/tyrosine ammonia lyase, cinnamate-4-hydroxlase, coumarate-CoA ligase and benzalacetone synthase, in an industrial strain of Saccharomyces cerevisiae. It is possible to produce sensorially-relevant quantities of raspberry ketone in the industrial heterologous host
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knobloch, K.H.; Hahlbrock, K.
4-Coumarate:CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm.
Arch. Biochem. Biophys.
184
237-248
1977
Petroselinum crispum
Manually annotated by BRENDA team
Douglas, C.; Hoffmann, H.; Schulz, W.; Hahlbrock, K.
Structure and elicitor or u.v.light -stimulated expression of two 4-coumarate:CoA ligase genes in parsley
EMBO J.
6
1189-1195
1987
Petroselinum crispum
Manually annotated by BRENDA team
Lee, D.; Lloyd, N.; Pretorius, I.; Borneman, A.
Heterologous production of raspberry ketone in the wine yeast Saccharomyces cerevisiae via pathway engineering and synthetic enzyme fusion
Microb. Cell Fact.
15
49
2016
Petroselinum crispum (P14913)
Manually annotated by BRENDA team