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Information on EC 2.3.1.217 - curcumin synthase and Organism(s) Curcuma longa and UniProt Accession C6L7V8

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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).
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This record set is specific for:
Curcuma longa
UNIPROT: C6L7V8
Word Map
The taxonomic range for the selected organisms is: Curcuma longa
The enzyme appears in selected viruses and cellular organisms
Synonyms
curcumin synthase, curcumin synthase 1, CURS, CURS1, CURS2, CURS3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
curcumin synthase
280731
-
curcumin synthase 1
298477
-
CURS
280731
-
CURS1
CURS2
CURS3
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
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).
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 + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
show the reaction diagram
preferred activity of CURS1, CURS2, and CURS3
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
show the reaction diagram
preferred activity of CURS1, CURS2, and CURS3
-
-
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
show the reaction diagram
preferred activity of CURS1, CURS2, and CURS3
-
-
?
cinnamoyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + dicinnamoylmethane + N-acetylcysteamine
show the reaction diagram
-
low activity
-
-
?
feruloyl-CoA + 3-oxo-5-phenyl-4-pentenoic acid + H2O
CoA + cinnamoylferuloylmethane + CO2
show the reaction diagram
-
-
-
?
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
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
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
(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
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
show the reaction diagram
C0SVZ6, C6L7V8, C6L7V9
preferred activity of CURS1, CURS2, and CURS3
-
-
?
(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
-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine
show the reaction diagram
C0SVZ6
-
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
show the reaction diagram
additional information
?
-
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
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0043
feruloyl-CoA
pH 7.5, 37C, CURS2
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
-
kinetic analysis of CURS, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068
feruloyl-CoA
pH 7.5, 37C, CURS2
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
1.622
feruloyl-CoA
pH 7.5, 37C, CURS2
0.112 - 20.54
3-oxo-5-phenyl-4-pentenoic acid
0.013 - 2.915
cinnamoyl-diketide-N-acetylcysteamine
1.001 - 2.017
feruloyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CURS2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
evolution
metabolism
-
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CURS2_CURLO
391
0
43146
Swiss-Prot
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
CURS2, DNA and amino acid sequence determination and analysis, expression analysis by quantitative real time PCR
CURS1, 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
-
expression of His4-tagged CURS1 in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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.
10
599-609
2015
Curcuma longa (C0SVZ6), Curcuma longa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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