Information on EC 2.3.1.218 - phenylpropanoylacetyl-CoA synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.218
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RECOMMENDED NAME
GeneOntology No.
phenylpropanoylacetyl-CoA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA
show the reaction diagram
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-
-
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feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO2 + CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
curcuminoid biosynthesis
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phenylphenalenone biosynthesis
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Stilbenoid, diarylheptanoid and gingerol biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)
The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
Curcuma sp.
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the Type III polyketide synthase family, but DCS is a unique type III PKS that releases the product as a CoA-bound form
metabolism
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the enzyme catalyzes a step in the curcuminoid biosynthesis, pathway overview
additional information
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DCS can collaborate with curcumin synthase, CURS, EC 2.3.1.217, which uses the reaction product feruloylacetyl-CoA for formation of curcumin, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + malonyl-CoA
(4-coumaroyl)acetyl-CoA + CO2 + CoA
show the reaction diagram
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-
-
-
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
show the reaction diagram
-
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product identification by LC-ESI MS/MS
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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
4-coumaroyl-CoA + malonyl-CoA
(4-coumaroyl)acetyl-CoA + CO2 + CoA
show the reaction diagram
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-
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-
?
feruloyl-CoA + malonyl-CoA
feruloylacetyl-CoA + CO2 + CoA
show the reaction diagram
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-
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0084
malonyl-CoA
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pH 7.5, 37°C, recombinant enzyme
additional information
additional information
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DCS is an allosteric enzyme. Homotropic activation decreases the activity as the substrate concentration decreases more quickly than those exhibiting Michaelis-Menten-type kinetics. Kinetic analysis of DCS, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
Feruloyl-CoA
Curcuma longa
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pH 7.5, 37°C, recombinant enzyme
0.0112
malonyl-CoA
Curcuma longa
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pH 7.5, 37°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 hide
LITERATURE
analysis