Information on EC 2.3.1.211 - bisdemethoxycurcumin synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.211
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RECOMMENDED NAME
GeneOntology No.
bisdemethoxycurcumin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 4-coumaroyl-CoA + malonyl-CoA + H2O = 3 CoA + bisdemethoxycurcumin + 2 CO2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Stilbenoid, diarylheptanoid and gingerol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)
A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoylacetyl-CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme's cavity and is not released to the environment.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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the enzyme is involved in the phenylpropanoid pathway. Thioesterase activities in Curcuma longa that cleave phenylpropanoid pathway CoA esters, are present at high levels in all tissues and may shunt phenylpropanoid pathway intermediates away from the production of curcuminoids and gingerols, thereby potentially playing a regulatory role in the biosynthesis of these compounds
additional information
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enzyme structure-function relationship, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 4-coumaroyl-CoA + malonyl-CoA + H2O
3 CoA + bisdemethoxycurcumin + 2 CO2
show the reaction diagram
2 cinnamoyl-CoA + malonyl-CoA + H2O
3 CoA + dicinnamoylmethane + 2 CO2
show the reaction diagram
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-
?
2 feruloyl-CoA + malonyl-CoA + H2O
3 CoA + 4-hydroxy-6-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-2H-pyran-2-one + curcumin
show the reaction diagram
very low activity
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-
?
2 feruloyl-CoA + malonyl-CoA + H2O
3 CoA + curcumin + 2 CO2
show the reaction diagram
4-coumaroyl-CoA + 3-oxodecanoyl-CoA
(1E,4Z)-5-hydroxy-1-(4-hydroxyphenyl)dodeca-1,4-dien-3-one + CoA
show the reaction diagram
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-
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?
4-coumaroyl-CoA + 3-oxooctanoyl-CoA
(1E,4Z)-5-hydroxy-1-(4-hydroxyphenyl)deca-1,4-dien-3-one + CoA
show the reaction diagram
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?
4-coumaroyl-CoA + 3-oxooctanoyl-CoA
(1E,4Z)-5-hydroxy-1-(4-hydroxyphenyl)hexadeca-1,4-dien-3-one + CoA
show the reaction diagram
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-
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-
?
4-coumaroyl-CoA + 3-oxooctanoyl-CoA
(1E,4Z)-5-hydroxy-1-(4-hydroxyphenyl)tetradeca-1,4-dien-3-one + CoA
show the reaction diagram
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?
4-coumaroyl-CoA + cinnamoyl-CoA + malonyl-CoA + H2O
3 CoA + cinnamoyl-4-coumaroyl-methane + 2 CO2
show the reaction diagram
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?
cinnamoyl-CoA + 2 malonyl-CoA + H2O
3 CoA + 4-hydroxy-6-[(E)-2-phenylethenyl]-2H-pyran-2-one + 2 CO2
show the reaction diagram
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cinnamoyl-CoA reacts to form a triketide pyrone with a small amount of dicinnamoylmethane
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?
cinnamoyl-CoA + 3-oxo-octanoate + H2O
CoA + cinnamoyl(hexanoyl)methane + ?
show the reaction diagram
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?
cinnamoyl-CoA + 3-oxo-octanoyl-N-acetylcysteamine thioester + H2O
CoA + cinnamoyl(hexanoyl)methane + ?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 4-coumaroyl-CoA + malonyl-CoA + H2O
3 CoA + bisdemethoxycurcumin + 2 CO2
show the reaction diagram
2 cinnamoyl-CoA + malonyl-CoA + H2O
3 CoA + dicinnamoylmethane + 2 CO2
show the reaction diagram
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?
2 feruloyl-CoA + malonyl-CoA + H2O
3 CoA + curcumin + 2 CO2
show the reaction diagram
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?
additional information
?
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the curcuminoid synthase might also use feruloyl-CoA as substrate, via demethoxycurcumin, to curcumin, possible pathway overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
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in vivo assay at
28
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
activity range, profile overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low activity
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme structure-function relationship, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, sitting drop vapour diffusion method, optimization of the crystallization conditions, mixing 0.0005 ml of protein solution, containing 10 mg/ml in 20 mM HEPES-NaOH, pH 7.0, 100 mM NaCl, and 2 mM DTT, with an equal volume of reservoir solution, containing 100 mM HEPES-NaOH, pH 7.8, 1995 mM ammonium sulfate, 3% dimethylsulfoxide, and 2 mM CoA, and equilibration against 0.1 ml reservoir solution, 20°C, cryoprotection in 100 mM HEPES-NaOH pH 7.8, 1330 mM ammonium sulfate, 2 mM CoA, 12% v/v glycerol and 14% w/v PEG 400, X-ray diffraction structure determination and analysis st 2.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3)
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity and anion exchange chromatography, followed by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ClPKS10, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, tissue expression analysis and quantification by real-time PCR
expression of the His-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene AK109558, expression of His6-tagged CUS in Escherichia coli strain BL21(DE3)-pLysS
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
engineering of an in vivo reporter assay for phenylalanine ammonia-lyase efficiency in Escherichia coli based on a plant type III polyketide biosynthetic pathway. The candidate phenylalanine ammonia-lyases are coexpressed with 4-coumarate:CoA ligase 4CL1 from Arabidopsis thaliana and curcuminoid synthase from Oryza sativa. A microplate-based assay is used to measure the titer of dicinnamoylmethane
synthesis
an engineered Escherichia coli strain expressing phenylalanine ammonia-lyase, 4-coumarate:CoA ligase 4CL1 from Arabidopsis thaliana and curcuminoid synthase from Oryza sativa leads to the production of dicinnamoylmethane at a high level of 0.36 g/l. Supplement of 2-fluoro-phenylalanine yields fluorinated dicinnamoylmethane derivatives, 6,6'-difluorodicinnamoylmethane and 6-fluoro-dicinnamoylmethane, of which the latter is a new curcuminoid