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Information on EC 2.3.1.218 - phenylpropanoylacetyl-CoA synthase
for references in articles please use BRENDA:EC2.3.1.218
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.218 phenylpropanoylacetyl-CoA synthase
IUBMB Comments
The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
The enzyme appears in viruses and cellular organisms
- 2.3.1.218
- curcuma
- longa
-
curcuminoids
- turmeric
- rhizome
-
ferulic
- feruloyl-coa
- synthesis
- 4-coumarate
- kwangsiensis
- demethoxycurcumin
-
3-hydroxylase
-
intraspecies
- ammonia
- caffeoyl-coa
- analysis
- bisdemethoxycurcumin
-
caffeic
- biofuel production
Reaction Schemes
showSynonyms
diketide-coa synthase, phenylpropanoylacetyl-coa synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DCS
diketide-CoA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA
-
-
-
-
feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO2 + CoA
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
curcuminoid biosynthesis, phenylphenalenone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)
The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + malonyl-CoA
(4-coumaroyl)acetyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: when diketide-CoA synthase (DCS) and curcumin synthase (ZoCURS) are co-incubated in the presence of 3-(4-hydroxyphenyl)propionyl-CoA and malonyl-CoA, tetrahydrobisdemethoxycurcumin and 4-hydroxybenzylacetone are produced
Products: -
Products: -
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
-
Substrates: -
Products: product identification by LC-ESI MS/MS
Products: product identification by LC-ESI MS/MS
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + malonyl-CoA
(4-coumaroyl)acetyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Confusion
Discrimination of Curcuma species from Asia using intron length polymorphism markers in genes encoding diketide-CoA synthase and curcumin synthase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
DCS is an allosteric enzyme. Homotropic activation decreases the activity as the substrate concentration decreases more quickly than those exhibiting Michaelis-Menten-type kinetics. Kinetic analysis of DCS, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the Type III polyketide synthase family, but DCS is a unique type III PKS that releases the product as a CoA-bound form
metabolism
-
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
-
DCS can collaborate with curcumin synthase, CURS, EC 2.3.1.217, which uses the reaction product feruloylacetyl-CoA for formation of curcumin, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85470
85470
diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3), SDS-PAGE
85470
diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3), SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a curcuminoid producing unnatural fusion protein diketide-CoA synthase:curcumin synthase is constructed
additional information
a curcuminoid producing unnatural fusion protein diketide-CoA synthase:curcumin synthase is constructed
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:curcumin synthase His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:curcumin synthase His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:curcumin synthase His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
DNA and amino acid sequence determination and analysis, expression analysis by quantitative real-time PCR, recombinant expression as N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
diketide-CoA synthase, curcumin synthase, and the unnatural fusion protein diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expressions of diketide-CoA synthase, curcumin synthase 3, and curcumin synthase (EC 2.3.1.217) are reduced by ethanol treatment
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biofuel production
incorporation of curcumin and phenylpentanoids into lignin has a positive effect on saccharification yield after alkaline pretreatment. To design a lignin that is easier to degrade under alkaline conditions, curcumin (diferuloylmethane) is produced in the model plant Arabidopsis thaliana via simultaneous expression of the turmeric genes diketide-CoA synthase (DCS) and curcumin synthase 2 (CURS2). The transgenic plants produce a plethora of curcumin- and phenylpentanoid-derived compounds with no negative impact on growth. Catalytic hydrogenolysis gives evidence that both curcumin and phenylpentanoids are incorporated into the lignifying cell wall, thereby significantly increasing saccharification efficiency after alkaline pretreatment of the transgenic lines by 14-24% as compared with the wild type
food industry
-
ethanol treatment attenuates the yellowing of fresh-cut yam stored at 25°C
synthesis
analysis
-
method for discriminating Curcuma species by intron length polymorphism markers in genes encoding diketide-CoA synthase and curcumin synthase. By applying this method, and constructing a dendrogram based on these markers, seven Curcuma species are clearly distinguishable and Curcuma longa specimens are geographically distinguishable
analysis
-
method to detect expression differences between species in detail, based on RNA sequencing analysis. The difference in the contents of curcuminoids among the species can be explained by the changes in the expression of genes encoding diketide-CoA synthase, and curcumin synthase at the branching point of the curcuminoid biosynthesis pathway
synthesis
a curcuminoid producing unnatural fusion protein diketide-CoA synthase:curcumin synthase is constructed. The fusion protein may contribute to further understand the biosynthesis of curcuminoids in ginger but also be advantage to further manipulate the biosynthesis of curcuminoid analogs, particularly including tetrahydrobisdemethoxycurcumin (THBDC) and various dihydrocurcuminoid derivatives in microorganisms
synthesis
design, construction and optimization of a heterologous pathway to produce curcuminoids in Escherichia coli. This pathway involves six enzymes, tyrosine ammonia lyase (TAL), 4-coumarate 3-hydroxylase (C3H), caffeic acid O-methyltransferase (COMT), 4-coumarate-CoA ligase (4CL), diketide-CoA synthase (DCS), and curcumin synthase (CURS1). Curcumin production is enhanced and reachs 43.2 mM, corresponding to an improvement of 160% comparing to mono-culture system
synthesis
a curcuminoid producing unnatural fusion protein diketide-CoA synthase:curcumin synthase is constructed. The fusion protein may contribute to further understand the biosynthesis of curcuminoids in ginger but also be advantage to further manipulate the biosynthesis of curcuminoid analogs, particularly including tetrahydrobisdemethoxycurcumin (THBDC) and various dihydrocurcuminoid derivatives in microorganisms
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katsuyama, Y.; Kita, T.; Funa, N.; Horinouchi, S.
Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa
J. Biol. Chem.
284
11160-11170
2009
Curcuma longa
brenda
Yang, E.; Gao, H.; Wu, Q.; Wang, F.
Gene cloning and sequence analysis of diketide CoA synthase in Amomum villosum
Chin. Tradit. Herbal Drugs
44
3037-3041
2013
Wurfbainia villosa (A0A0U1WZ71)
-
brenda
Kita, T.; Komatsu, K.; Zhu, S.; Iida, O.; Sugimura, K.; Kawahara, N.; Taguchi, H.; Masamura, N.; Cai, S.Q.
Development of intron length polymorphism markers in genes encoding diketide-CoA synthase and curcumin synthase for discriminating Curcuma species
Food Chem.
194
1329-1336
2016
Curcuma
brenda
Li, D.; Ono, N.; Sato, T.; Sugiura, T.; Altaf-Ul-Amin, M.; Ohta, D.; Suzuki, H.; Arita, M.; Tanaka, K.; Ma, Z.; Kanaya, S.
Targeted integration of RNA-Seq and metabolite data to elucidate curcuminoid biosynthesis in four Curcuma species
Plant Cell Physiol.
56
843-851
2015
Curcuma longa
brenda
Zhang, L.; Gao, B.; Wang, X.; Zhang, Z.; Liu, X.; Wang, J.; Mo, T.; Liu, Y.; Shi, S.; Tu, P.
Identification of a new curcumin synthase from ginger and construction of a curcuminoid-producing unnatural fusion protein diketide-CoA synthase - curcumin synthase
RSC Adv.
6
12519-12524
2016
Curcuma longa (C0SVZ5), Zingiber officinale (A5GZV8)
-
brenda
Jiang, Y.; Liao, Q.; Zou, Y.; Liu, Y.; Lan, J.
Transcriptome analysis reveals the genetic basis underlying the biosynthesis of volatile oil, gingerols, and diarylheptanoids in ginger (Zingiber officinale Rosc.)
Bot. Stud.
58
41
2017
Zingiber officinale
brenda
Rodrigues, J.L.; Gomes, D.; Rodrigues, L.R.
A combinatorial approach to optimize the production of curcuminoids from tyrosine in Escherichia coli
Front. Bioeng. Biotechnol.
8
59
2020
Curcuma longa (C0SVZ5)
brenda
Oyarce, P.; De Meester, B.; Fonseca, F.; de Vries, L.; Goeminne, G.; Pallidis, A.; De Rycke, R.; Tsuji, Y.; Li, Y.; Van den Bosch, S.; Sels, B.; Ralph, J.; Vanholme, R.; Boerjan, W.
Introducing curcumin biosynthesis in Arabidopsis enhances lignocellulosic biomass processing
Nat. Plants
5
225-237
2019
Curcuma longa (C0SVZ5), Curcuma longa
brenda
Guo, S.; Zhao, X.; Ma, Y.; Zhang, Y.; Wang, D.
Ethanol treatment suppresses the yellowing of fresh-cut yam by repressing the phenylpropanoid pathway and bisdemethoxycurcumin biosynthesis
Postharvest Biol. Technol.
181
111642
2021
Dioscorea oppositifolia
-
brenda
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