Identification and characterization of multiple curcumin synthases from the herb <i>Curcuma longa</i>

Katsuyama, Yoshihiko; Kita, Tomoko; Horinouchi, Sueharu

doi:10.1016/j.febslet.2009.07.029

Cited by 98 publications

(83 citation statements)

References 16 publications

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“…DCS and CURS1 were also chosen to test the curcuminoids production due to the promising results previously reported in vitro [9,10,16]. Although these two genes were successfully expressed in E. coli and the enzymes were used to produce several curcuminoids, including curcumin, DCS and CURS1 were never tested in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…CURS2 was also reported to prefer feruloylCoA and CURS3 favored both feruloy-CoA and p-coumaroyl-CoA [10]. Since curcumin has been reported to possess, in some systems, a higher therapeutic value than the other curcuminoids [17], CURS1 was chosen as it has the highest turnover rate towards feruloyl-CoA, as well as the highest difference between the catalytic efficiency towards feruloyl-CoA and p-coumaroyl-CoA [10].…”

Section: Discussionmentioning

confidence: 99%

“…After CUS was discovered, Katsuyama et al [9] reported that in the C. longa plant, the PKSs used to produce curcuminoids were diketide-CoA synthase (DCS) and curcumin synthase (CURS1). They also identified other CURS enzymes (CURS2 and CURS3) with different substrate specificities [10]. It is important to bear in mind that CUS catalyzes both steps that are catalyzed separately by DCS and CURS [9] (Fig.…”

Section: Introductionmentioning

confidence: 98%

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Production of curcuminoids from tyrosine by a metabolically engineered Escherichia coli using caffeic acid as an intermediate

Rodrigues

Araújo

Prather

et al. 2015

Biotechnology Journal

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Curcuminoids are phenylpropanoids with high pharmaceutical potential. Herein, we report an engineered artificial pathway in Escherichia coli to produce natural curcuminoids through caffeic acid. Arabidopsis thaliana 4-coumaroyl-CoA ligase (4CL1) and Curcuma longa diketide-CoA synthase (DCS) and curcumin synthase (CURS1) were used to produce curcuminoids and 70 mg/L of curcumin was obtained from ferulic acid. Bisdemethoxycurcumin and demethoxycurcumin were also produced, but in lower concentrations, by feeding p-coumaric acid or a mixture of p-coumaric acid and ferulic acid, respectively. Additionally, curcuminoids were produced from tyrosine through the caffeic acid pathway. To produce caffeic acid, tyrosine ammonia lyase (TAL) from Rhodotorula glutinis and 4-coumarate 3-hydroxylase (C3H) from Saccharothrix espanaensis were used. Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) from Medicago sativa was used to convert caffeoyl-CoA to feruloyl-CoA.Using caffeic acid, p-coumaric acid or tyrosine as a substrate, 3.9 mg/L, 0.3 mg/L and 0.2 mg/L of curcumin were produced, respectively. This is the first time DCS and CURS1 were used in vivo to produce curcuminoids and that curcumin was produced by feeding tyrosine. We have shown that curcumin can be produced using a pathway through caffeic acid. This alternative pathway represents a step forward in the heterologous production of curcumin using E. coli.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Production of curcuminoids from tyrosine by a metabolically engineered Escherichia coli using caffeic acid as an intermediate

Rodrigues

Araújo

Prather

et al. 2015

Biotechnology Journal

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“…CURS2 uses feruloyl-CoA as a preferred starter substrate, and CURS3 prefers both feruloyl-CoA and 4-coumaroyl-CoA. Based on their substrate preference, CURS2 can synthesize curcumin and demethoxycurcumin, whereas CURS3 may synthesize curcumin, bisdemethoxycurcumin, and demethoxycurcumin (18). The presence of three similar enzymes and their substrate specificity may explain the natural mixture of these curcuminoids from C. longa.…”

Section: Plant Type III Pkssmentioning

confidence: 99%

Type III polyketide synthases in natural product biosynthesis

et al. 2012

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SummaryPolyketides represent an important class of biologically active and structurally diverse compounds in nature. They are synthesized from acyl-coenzyme A substrates by polyketide synthases (PKSs). PKSs are classified into three groups: types I, II, and III. This article introduces recent studies on type III PKSs identified from plants, bacteria, and fungi, and describes the catalytic functions of these enzymes in detail. Plant type III PKSs have been widely studied, as exemplified by chalcone synthase, which plays an important role in the synthesis of plant metabolites. Bacterial type III PKSs fall into five groups, many of which were identified from Streptomyces, a genus that has been well known for its production of bioactive molecules and genetic alterability. Although it was believed that type III PKSs exist exclusively in plants and bacteria, recent fungal genome sequencing projects and biochemical studies revealed the presence of type III PKSs in filamentous fungi, which provides a new chance to study fungal secondary metabolism and synthesize ''unnatural'' natural products. Type III PKSs have been used for the biosynthesis of novel molecules through precursordirected and structure-based mutagenesis approaches.2012 IUBMB IUBMB Life, 64(4): [285][286][287][288][289][290][291][292][293][294][295] 2012

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“…The same authors identified and characterized two other type III PKS from turmeric, named CURS2 and CURS3 (102). In vitro analysis revealed that CURS2 preferred feruloyl-CoA as the substrate, while CURS3 used both feruloyl-CoA and p-coumaroylCoA (Table 2).…”

Section: Curcuminoid Production In Curcuma Longamentioning

confidence: 99%

Heterologous Production of Curcuminoids

Rodrigues

Prather

Kluskens

et al. 2015

Microbiol Mol Biol Rev

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SUMMARY Curcuminoids, components of the rhizome of turmeric, show several beneficial biological activities, including anticarcinogenic, antioxidant, anti-inflammatory, and antitumor activities. Despite their numerous pharmaceutically important properties, the low natural abundance of curcuminoids represents a major drawback for their use as therapeutic agents. Therefore, they represent attractive targets for heterologous production and metabolic engineering. The understanding of biosynthesis of curcuminoids in turmeric made remarkable advances in the last decade, and as a result, several efforts to produce them in heterologous organisms have been reported. The artificial biosynthetic pathway (e.g., in Escherichia coli ) can start with the supplementation of the amino acid tyrosine or phenylalanine or of carboxylic acids and lead to the production of several natural curcuminoids. Unnatural carboxylic acids can also be supplemented as precursors and lead to the production of unnatural compounds with possibly novel therapeutic properties. In this paper, we review the natural conversion of curcuminoids in turmeric and their production by E. coli using an artificial biosynthetic pathway. We also explore the potential of other enzymes discovered recently or already used in other similar biosynthetic pathways, such as flavonoids and stilbenoids, to increase curcuminoid yield and activity.

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Identification and characterization of multiple curcumin synthases from the herb Curcuma longa

Cited by 98 publications

References 16 publications

Production of curcuminoids from tyrosine by a metabolically engineered Escherichia coli using caffeic acid as an intermediate

Production of curcuminoids from tyrosine by a metabolically engineered Escherichia coli using caffeic acid as an intermediate

Type III polyketide synthases in natural product biosynthesis

Heterologous Production of Curcuminoids

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