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Information on EC 2.3.1.217 - curcumin synthase
for references in articles please use BRENDA:EC2.3.1.217
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.217 curcumin synthase
IUBMB Comments
A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well (see EC 2.3.1.219, demethoxycurcumin synthase).
The enzyme appears in viruses and cellular organisms
- 2.3.1.217
- curcuma
-
diketide-coa
- longa
-
curcuminoids
- rhizome
- turmeric
- synthesis
- polyketide
- demethoxycurcumin
- bisdemethoxycurcumin
-
ferulic
- 4-coumarate
-
zingiberaceae
- zedoaria
-
condensing
-
intraspecies
- caffeoyl-coa
- kwangsiensis
-
3-hydroxylase
- analysis
- biofuel production
showSynonyms
curs1, curs3, curcumin synthase, curs2, curcumin synthase 1, curcumin synthase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CURS
CURS1
CURS2
CURS3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)
A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).
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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)acetyl-CoA + 3-(4-hydroxyphenyl)propionyl-CoA + H2O
2 CoA + tetrahydrobisdemethoxycurcumin + CO2
Substrates: -
Products: -
Products: -
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
Substrates: preferred activity of CURS1, CURS2, and CURS3
Products: -
Products: -
?
4-methoxyferuloyl-CoA + 4-methoxyferuloylacetyl-CoA + H2O
2 CoA + dimethylcurcumin + CO2
-
Substrates: -
Products: -
Products: -
?
cinnamoyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + dicinnamoylmethane + N-acetylcysteamine
-
Substrates: low activity
Products: -
Products: -
?
dihydro-4-coumaroyl-CoA + 4-coumaroylacetyl-CoA + H2O
2 CoA + dihydrobisdemethoxycurcumin + CO2
-
Substrates: -
Products: -
Products: -
?
dihydroferuloyl-CoA + 4-coumaroylacetyl-CoA + H2O
2 CoA + dihydrodemethoxycurcumin + CO2
-
Substrates: -
Products: -
Products: -
?
dihydroferuloyl-CoA + dihydroferuloylacetyl-CoA + H2O
2 CoA + tetrahydrocurcumin + CO2
-
Substrates: -
Products: -
Products: -
?
dihydroferuloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + dihydrocurcumin + CO2
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + 3-oxo-5-phenyl-4-pentenoic acid + H2O
CoA + cinnamoylferuloylmethane + CO2
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
Substrates: via 3-oxo-5-phenyl-4-pentenoic acid
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: preferred activity of CURS1, CURS2, and CURS3
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
Substrates: feruloyl-CoA is the preferred starter substrate
Products: product identification by LC-ESI MS/MS
Products: product identification by LC-ESI MS/MS
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: two-step reaction of hydrolysis and decarboxylative condensation
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: CURS1 catalyzes the hydrolysis of diketide-CoA to yield a 2-oxoacid (ii) and decarboxylative condensation of the 2-oxoacid with feruloyl-CoA to yield curcumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can also convert diketide-CoA esters into 2-oxoacids and CoA, which are then converted into curcuminoids. For activity assays, cinnamoyl-CoA, 4-coumaroyl-CoA, or feruloyl-CoA are used as starter substrates and malonyl-CoA or cinnamoyl-diketide-N-acetylcysteamine as extender substrates, cf. EC 2.3.1.218 and EC 2.31.219
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA, cf. EC 2.3.1.219. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA, cf. EC 2.3.1.219. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA, cf. EC 2.3.1.219. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA, cf. EC 2.3.1.219. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, while CURS3 is equally active with both feruloyl-CoA and 4-coumaroyl-CoA. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PKS2 accepts p-coumaric acid, dihydrocoumaric acid, and ferulic acid as substrates but not dihydroferulic acid, while isoform PKS1 utilizes dihydrocoumaric acid, ferulic acid and dihydro-ferulic acid but not p-coumaric acid
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: -
?
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: -
?
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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)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
Substrates: preferred activity of CURS1, CURS2, and CURS3
Products: -
Products: -
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: CURS1 catalyzes the hydrolysis of diketide-CoA to yield a 2-oxoacid (ii) and decarboxylative condensation of the 2-oxoacid with feruloyl-CoA to yield curcumin
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
Substrates: preferred activity of CURS1, CURS2, and CURS3
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
-
kinetic analysis of CURS, overview
-
0.0012
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant H303Q
0.0059
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant wild-type enzyme
0.138
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant G211F
0.0017
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant wild-type enzyme
0.003
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant H303Q
0.113
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant G211F
0.018
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant H303Q
0.0083
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant G211F
0.125
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant wild-type enzyme
0.00007
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant H303Q
0.0015
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant G211F
0.0043
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant wild-type enzyme
0.0183
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.112
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant G211F
1.605
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant H303Q
20.54
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant wild-type enzyme
0.013
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant G211F
0.024
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant H303Q
2.915
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
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
metabolism
physiological function
expression of diketide-CoA synthase DCS and curcumin synthase CURS3 in Atropa belladonna results in the production of curcumin and its glucoside
additional information
evolution
the enzyme belongs to the type III polyketide synthase family. A Cys-His-Asn catalytic triad is conserved in all known type III polyketide synthases
evolution
the enzyme belongs to the Type III polyketide synthase family. A Cys-His-Asn catalytic triad is conserved in all known type III PKSs
metabolism
-
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
metabolism
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
-
CURS can collaborate with curcumin synthase, DCS, EC 2.3.1.218, which provides the substrate feruloylacetyl-CoA from condensation of feruloyl-CoA and malonyl-CoA, overview
additional information
active site residue His303 is important for 2-oxoacid condensation, involvement of the hydrophobic cavity around Phe265 in 2-oxoacid condensation, wild-type and mutant ligand binding structures and structure-function relationship, modeling, 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). CURS3_CURLO
390
0
43099
Swiss-Prot
Secretory Pathway (Reliability: 1)
CUS_ORYSJ
402
0
43212
Swiss-Prot
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85470
diketide-CoA synthase:CURS His-tagged at their N terminus are produced in Escherichia coli BL21 (DE3), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
residue S146 is predicted to be a phosphorylation site
phosphoprotein
residue S196 is predicted to be a phosphorylation site
phosphoprotein
residue S33 is predicted to be a phosphorylation site
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His4-tagged CURS1, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 10% glycerol, and 1 mM tris(2-carboxyethyl)phosphine with reservoir solution containing 0.3 M sodium malonate, pH 7.0, and 25% PEG3350, X-ray diffraction structure determination and analysis at 2.32 A resolution, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G211F
site-directed mutagenesis, the mutant shows highly reduced 2-oxoacid condensation activity compared to the wild-type enzyme
H303A
site-directed mutagenesis, active site residue mutant, the mutant shows reduced 2-oxoacid condensation activity compared to the wild-type enzyme
H303Q
site-directed mutagenesis, active site residue mutant, the mutant shows reduced 2-oxoacid condensation activity compared to the wild-type enzyme
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)
recombinant His4-tagged CURS1 from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CURS1, DNA and amino acid sequence determination and analysis, expression analysis by quantitative real time PCR
CURS2, DNA and amino acid sequence determination and analysis, expression analysis by quantitative real time PCR
CURS3, DNA and amino acid sequence determination and analysis, expression analysis by quantitative real time PCR
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)
-
PAL (phenylalanine ammonia lyase) or TAL (tyrosine ammonia lyase), along with Os4CL (p-coumaroyl-CoA ligase) and CUS (curcumin synthase) genes, are introduced into Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expressions of diketide-CoA synthase (EC 2.3.1.218), curcumin synthase 3, and curcumin synthase 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
analysis
-
classification of Curcuma species based on the intron length polymorphism markers in genes encoding diketide-CoA synthase and curcumin synthase and the trnK intron sequences
synthesis
production of curcuminoids using an engineered artificial pathway in Escherichia coli. Expression of Arabidopsis thaliana 4-coumaroyl-CoA ligase and Curcuma longa diketide-CoA synthase (DCS) and curcumin synthase (CURS1) leads to synthesis of 70 mg/l of curcumin from ferulic acid. Bisdemethoxycurcumin and demethoxycurcumin are produced, but in lower concentrations, by feeding 4-coumaric acid or a mixture of 4-coumaric acid and ferulic acid, respectively. To produce caffeic acid, tyrosine ammonia lyase from Rhodotorula glutinis and 4-coumarate 3-hydroxylase from Saccharothrix espanaensis are used. Caffeoyl-CoA 3-O-methyltransferase from Medicago sativa converts caffeoyl-CoA to feruloyl-CoA. Using caffeic acid, 4-coumaric acid or tyrosine as a substrate, 3.9, 0.3, and 0.2 mg/l of curcumin are produced, respectively
synthesis
construction of a fusion protein diketide-CoA synthase::curcumin synthase. Comparing to CURS, the fusion protein shows similar substrate specificities and catalytic potentials to catalyze the formation of various curcuminoids, with increased yields of curcuminoids
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
production of curcuminoids in engineered Escherichia coli. Two curcuminoids (dicinnamoylmethane and bisdemethoxycurcumin) are synthesized from glucose in Escherichia coli. PAL (phenylalanine ammonia lyase) or TAL (tyrosine ammonia lyase), along with Os4CL (p-coumaroyl-CoA ligase) and CUS (curcumin synthase) genes, are introduced into Escherichia coli, and each strain produces dicinnamoylmethane or bisdemethoxycurcumin, respectively. In order to increase the production of curcuminoids in Escherichia coli, the shikimic acid biosynthesis pathway, which increases the substrates for curcuminoid biosynthesis, is engineered. Using the engineered strains, the production of bisdemethoxycurcumin increases from 0.32 to 4.63 mg/l, and that of dicinnamoylmethane from 1.24 to 6.95 mg/l
synthesis
biosynthetic pathway of p-coumaric acid, caffeic acid and curcumin in Escherichia coli can be triggered by using heat shock promoters, suggesting its potential for the development of new industrial bioprocesses or even new bacterial therapies. p-Coumaric acid is successfully produced from tyrosine and caffeic acid produced either from tyrosine or p-coumaric acid using tyrosine ammonia lyase (TAL) from Rhodotorula glutinis, 4-coumarate 3-hydroxylase (C3H) from Saccharothrix espanaensis or cytochrome P450 CYP199A2 from Rhodopseudomonas palustris. The highest p-coumaric acid production obtained is 2.5 mM. Caffeic acid production reaches 0.370 mM. 0.017 mM cumin is produced using 4-coumarate-CoA ligase (4CL1) from Arabidopsis thaliana, diketide-CoA synthase (DCS) and curcumin synthase 1 (CURS1) from Curcuma longa
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
expression of diketide-CoA synthase DCS and curcumin synthase CURS3 in Atropa belladonna results in the production of curcumin and its glucoside. Under shake-flask cultivation, a maximum curcumin yield of 180.62 microg/g dry weight is observed. A content of curcumin monoglucoside of 32.63 mictog/g dry weight along with 67.89 microg/g dry weight curcumin is noted upon additional expression of Curcuma amada glucosyltransferase UGT2 genes
synthesis
engineering Saccharomyces cerevisiae to produce curcumin from glucose by using 4-hydroxyphenylacetate 3-monooxygenase oxygenase complex from Pseudomonas aeruginosa and Salmonella enterica, caffeic acid O-methyltransferase from Arabidopsis thaliana, feruloyl-CoA synthetase from Pseudomonas paucimobilis, and diketide-CoA synthase and curcumin synthase from Curcuma longa in a 4-coumaric acid overproducing S. cerevisiae strain. Following optimization, a strain capable of producing 4.2 mg/l is obtained
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katsuyama, Y.; Kita, T.; Horinouchi, S.
Identification and characterization of multiple curcumin synthases from the herb Curcuma longa
FEBS Lett.
583
2799-2803
2009
Curcuma longa (C0SVZ6), Curcuma longa (C6L7V8), Curcuma longa (C6L7V9), Curcuma longa
brenda
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
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2009
Curcuma longa
brenda
Katsuyama, Y.; Miyazono, K.; Tanokura, M.; Ohnishi, Y.; Horinouchi, S.
Structural and biochemical elucidation of mechanism for decarboxylative condensation of beta-keto acid by curcumin synthase
J. Biol. Chem.
286
6659-6668
2011
Curcuma longa (C0SVZ6)
brenda
Rodrigues, J.L.; Araujo, R.G.; Prather, K.L.; Kluskens, L.D.; Rodrigues, L.R.
Production of curcuminoids from tyrosine by a metabolically engineered Escherichia coli using caffeic acid as an intermediate
Biotechnol. J.
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2015
Curcuma longa (C0SVZ6), Curcuma longa
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
Zingiber officinale, Zingiber officinale (A5GZV8)
-
brenda
Rodrigues, J.; Couto, M.; Arajo, R.; Prather, K.; Kluskens, L.; Rodrigues, L.
Hydroxycinnamic acids and curcumin production in engineered Escherichia coli using heat shock promoters
Biochem. Eng. J.
125
41-49
2017
Curcuma longa (C0SVZ6)
-
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 (C0SVZ6)
brenda
Kim, E.J.; Cha, M.N.; Kim, B.G.; Ahn, J.H.
Production of curcuminoids in engineered Escherichia coli
J. Microbiol. Biotechnol.
27
975-982
2017
Oryza sativa Japonica Group (Q8LIL0)
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 (C6L7V8), Curcuma longa
brenda
Sandeep, I.S.; Das, S.; Nasim, N.; Mishra, A.; Acharya, L.; Joshi, R.K.; Nayak, S.; Mohanty, S.
Differential expression of CURS gene during various growth stages, climatic condition and soil nutrients in turmeric (Curcuma longa) Towards site specific cultivation for high curcumin yield
Plant Physiol. Biochem.
118
348-355
2017
Curcuma longa (C0SVZ6), Curcuma longa
brenda
Rainha, J.; Rodrigues, J.L.; Rodrigues, L.R.
De novo biosynthesis of curcumin in Saccharomyces cerevisiae
ACS Synth. Biol.
13
1727-1736
2024
Curcuma longa (C0SVZ6)
brenda
Singh, S.; Pandey, P.; Akhtar, M.Q.; Negi, A.S.; Banerjee, S.
A new synthetic biology approach for the production of curcumin and its glucoside in Atropa belladonna hairy roots
J. Biotechnol.
328
23-33
2021
Curcuma amada (A0A1X9IAM8)
brenda
Santhoshkumar, R.; Yusuf, A.
In silico structural modeling and analysis of physicochemical properties of curcumin synthase (CURS1, CURS2, and CURS3) proteins of Curcuma longa
J. Genet. Eng. Biotechnol.
18
24
2020
Curcuma longa (C0SVZ6), Curcuma longa (C6L7V8), Curcuma longa (C6L7V9)
brenda
Liu, Q.; Zhu, S.; Hayashi, S.; Iida, O.; Takano, A.; Miyake, K.; Sukrong, S.; Agil, M.; Balachandran, I.; Nakamura, N.; Kawahara, N.; Komatsu, K.
Discrimination of Curcuma species from Asia using intron length polymorphism markers in genes encoding diketide-CoA synthase and curcumin synthase
J. Nat. Med.
76
69-86
2022
Curcuma sp.
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
Chen, R.; Hu, T.; Wang, M.; Hu, Y.; Chen, S.; Wei, Q.; Yin, X.; Xie, T.
Functional characterization of key polyketide synthases by integrated metabolome and transcriptome analysis on curcuminoid biosynthesis in Curcuma wenyujin
Synth. Syst. Biotechnol.
7
849-861
2022
Curcuma wenyujin
brenda
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