Information on EC 2.3.1.217 - curcumin synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.217
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RECOMMENDED NAME
GeneOntology No.
curcumin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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curcuminoid biosynthesis
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Stilbenoid, diarylheptanoid and gingerol biosynthesis
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Curcuma sp.
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4-coumaroyl)acetyl-CoA + 3-(4-hydroxyphenyl)propionyl-CoA + H2O
2 CoA + tetrahydrobisdemethoxycurcumin + CO2
show the reaction diagram
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-
-
-
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
show the reaction diagram
preferred activity of CURS1, CURS2, and CURS3
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-
?
cinnamoyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + dicinnamoylmethane + N-acetylcysteamine
show the reaction diagram
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low activity
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-
?
feruloyl-CoA + 3-oxo-5-phenyl-4-pentenoic acid + H2O
CoA + cinnamoylferuloylmethane + CO2
show the reaction diagram
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-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine
show the reaction diagram
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
show the reaction diagram
via 3-oxo-5-phenyl-4-pentenoic acid
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-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
show the reaction diagram
C0SVZ6, C6L7V8, C6L7V9
preferred activity of CURS1, CURS2, and CURS3
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-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine
show the reaction diagram
C0SVZ6
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-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
show the reaction diagram
additional information
?
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C0SVZ6
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.138
3-oxo-5-phenyl-4-pentenoic acid
0.0017 - 0.113
cinnamoyl-diketide-N-acetylcysteamine
0.0022 - 0.018
Feruloyl-CoA
additional information
additional information
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kinetic analysis of CURS, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.125
3-oxo-5-phenyl-4-pentenoic acid
0.00007 - 0.0043
cinnamoyl-diketide-N-acetylcysteamine
0.0032 - 0.0183
Feruloyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.112 - 20.54
3-oxo-5-phenyl-4-pentenoic acid
12236
0.013 - 2.915
cinnamoyl-diketide-N-acetylcysteamine
7946
1.001 - 2.017
Feruloyl-CoA
427
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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assay at
7.5
assay at; assay at; assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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)
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expression in Escherichia coli
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expression of His4-tagged CURS1 in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G211F
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site-directed mutagenesis, the mutant shows highly reduced 2-oxoacid condensation activity compared to the wild-type enzyme
H303A
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site-directed mutagenesis, active site residue mutant, the mutant shows reduced 2-oxoacid condensation activity compared to the wild-type enzyme
H303Q
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site-directed mutagenesis, active site residue mutant, the mutant shows reduced 2-oxoacid condensation activity compared to the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis