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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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2.3.1.217 curcumin synthaseIUBMB 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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Word Map
- 2.3.1.217
- curcuma
-
diketide-coa
- longa
-
curcuminoids
- rhizome
- turmeric
- synthesis
- polyketide
- demethoxycurcumin
- bisdemethoxycurcumin
-
ferulic
- 4-coumarate
-
zingiberaceae
- zedoaria
-
condensing
-
intraspecies
- caffeoyl-coa
- kwangsiensis
-
3-hydroxylase
- analysis
- biofuel production
The taxonomic range for the selected organisms is: Curcuma longa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
curs1, curs3, curcumin synthase, curs2, curcumin synthase 1, curcumin synthase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CURS1
CURS3
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
preferred activity of CURS1, CURS2, and CURS3
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
preferred activity of CURS1, CURS2, and CURS3
-
-
?
(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 + 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
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
-
-
?
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
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
preferred activity of CURS1, CURS2, and CURS3
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
preferred activity of CURS1, CURS2, and CURS3
-
-
?
(4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O
demethoxycurcumin + CO2 + 2 CoA
preferred activity of CURS1, CURS2, and CURS3
-
-
?
feruloyl-CoA + cinnamoyl-diketide-N-acetylcysteamine + H2O
CoA + cinnamoylferuloylmethane + N-acetylcysteamine + 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
-
-
?
feruloyl-CoA + feruloylacetyl-CoA + H2O
2 CoA + curcumin + CO2
preferred activity of CURS1, CURS2, and CURS3
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.018
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0183
feruloyl-CoA
-
pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.112
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant G211F
1.605
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant mutant H303Q
20.54
3-oxo-5-phenyl-4-pentenoic acid
pH 7.5, 37°C, recombinant wild-type enzyme
0.013
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant G211F
0.024
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant mutant H303Q
2.915
cinnamoyl-diketide-N-acetylcysteamine
pH 7.5, 37°C, recombinant wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
additional information
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
the enzyme belongs to the type III polyketide synthase family. A Cys-His-Asn catalytic triad is conserved in all known type III polyketide synthases
metabolism
-
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
metabolism
the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
active site residue His303 is important for 2-oxoacid condensation, involvement of the hydrophobic cavity around Phe265 in 2-oxoacid condensation, wild-type and mutant ligand binding structures and structure-function relationship, modeling, overview
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
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). CURS2_CURLO
391
0
43146
Swiss-Prot
Mitochondrion (Reliability: 4)
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
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)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
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
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
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
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
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)
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
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
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)
-
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)
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
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
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