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Information on EC 2.3.1.219 - demethoxycurcumin synthase
for references in articles please use BRENDA:EC2.3.1.219
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.219 demethoxycurcumin 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 (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
curcumin synthase, CURS, CURS1, CURS2, CURS3, ZoCURS, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CURS3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2
(2)
4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2
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4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
(1)
4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-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 (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].
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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 + 4-coumaroyl-CoA + H2O
bisdemethoxycurcumin + 2 CO2 + CoA
Substrates: preferred activity of CURS3
Products: -
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(4-coumaroyl)acetyl-CoA + 4-coumaroyl-CoA + H2O
bisdemethoxycurcumin + CO2 + CoA
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Substrates: -
Products: -
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(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + CoA
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Substrates: -
Products: -
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4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O
2 CoA + bidemethoxycurcumin + CO2
Substrates: curcumin synthase (ZoCURS), in the presence of diketide-CoA synthase, can accept p-coumaroyl-CoA to produce bidemethoxycurcumin
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4-coumaroyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoyl-4-coumaroylmethane + N-acetylcysteamine
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Substrates: -
Products: -
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cinnamoyl-CoA + cinnamoyl-acetyl-CoA + H2O
2 CoA + dicinnamoylmethane + CO2
Substrates: curcumin synthase (ZoCURS), in the presence of diketide-CoA synthase, can accept cinnamoyl-CoA to produce dicinnamoylmethane
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cinnamoyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + dicinnamoylmethane + N-acetylcysteamine
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Substrates: low activity
Products: -
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4-coumaroyl-CoA + feruloylacetyl-CoA
demethoxycurcumin + CO2 + CoA
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Substrates: -
Products: -
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4-coumaroyl-CoA + feruloylacetyl-CoA
demethoxycurcumin + CO2 + CoA
Substrates: preferred activity of CURS3
Products: -
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additional information
?
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Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, cf. EC 2.3.1.217, 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: -
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additional information
?
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Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, cf. EC 2.3.1.217, 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: -
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additional information
?
-
Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, cf. EC 2.3.1.217, 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: -
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additional information
?
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Substrates: substrate specificity, overview. CURS2 prefers feruloyl-CoA as a starter substrate, cf. EC 2.3.1.217, 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: -
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additional information
?
-
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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 2.3.1.217. 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 2.3.1.217. 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 2.3.1.217. 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 2.3.1.217. Thus, CURS2 synthesizes curcumin or demethoxycurcumin and CURS3 synthesizes curcumin, bisdemethoxycurcumin and demethoxycurcumin
Products: -
Products: -
?
additional information
?
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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
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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 + 4-coumaroyl-CoA + H2O
bisdemethoxycurcumin + 2 CO2 + CoA
Substrates: preferred activity of CURS3
Products: -
Products: -
?
(4-coumaroyl)acetyl-CoA + 4-coumaroyl-CoA + H2O
bisdemethoxycurcumin + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + CoA
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Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + feruloylacetyl-CoA
demethoxycurcumin + CO2 + CoA
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Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + feruloylacetyl-CoA
demethoxycurcumin + CO2 + CoA
Substrates: preferred activity of CURS3
Products: -
Products: -
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis of CURS, overview
-
0.085
4-coumaroyl-CoA
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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
3.15
4-coumaroyl-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
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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
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the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
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
-
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
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
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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). A5GZV8_ZINOF
390
0
43236
TrEMBL
other Location (Reliability: 2)
CURS1_CURLO
389
0
43034
Swiss-Prot
other Location (Reliability: 4)
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
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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)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
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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, Curcuma longa (C0SVZ6), Curcuma longa (C6L7V8), Curcuma longa (C6L7V9)
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
11160-11170
2009
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 (A5GZV8)
-
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 (C6L7V9)
brenda
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