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(4-coumaroyl)acetyl-CoA + 3-(4-hydroxyphenyl)propionyl-CoA + H2O
2 CoA + tetrahydrobisdemethoxycurcumin + CO2
-
-
-
-
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
preferred activity of CURS1, CURS2, and CURS3
-
-
?
cinnamoyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + dicinnamoylmethane + N-acetylcysteamine
-
low activity
-
-
?
feruloyl-CoA + 3-oxo-5-phenyl-4-pentenoic acid + H2O
CoA + cinnamoylferuloylmethane + CO2
-
-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
additional information
?
-
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
-
-
-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
-
-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + CO2
via 3-oxo-5-phenyl-4-pentenoic acid
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
-
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
preferred activity of CURS1, CURS2, and CURS3
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
feruloyl-CoA is the preferred starter substrate
product identification by LC-ESI MS/MS
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
two-step reaction of hydrolysis and decarboxylative condensation
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
-
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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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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
-
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
0.0022
feruloyl-CoA
pH 7.5, 37°C, CURS3
0.0043
feruloyl-CoA
pH 7.5, 37°C, CURS2
0.018
feruloyl-CoA
pH 7.5, 37°C, CURS1
0.018
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
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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
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
0.0032
feruloyl-CoA
pH 7.5, 37°C, CURS3
0.0068
feruloyl-CoA
pH 7.5, 37°C, CURS2
0.0183
feruloyl-CoA
pH 7.5, 37°C, CURS1
0.0183
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
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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
analysis
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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
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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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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
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
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
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
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
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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
11160-11170
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.
10
599-609
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
-
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
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