Information on EC 2.3.1.212 - benzalacetone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.212
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RECOMMENDED NAME
GeneOntology No.
benzalacetone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
raspberry ketone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (4-hydroxybenzalacetone-forming)
A polyketide synthase that catalyses the C6-C4 skeleton of phenylbutanoids in higher plants.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 (2RS)-methylmalonyl-CoA + H2O
6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone + ?
show the reaction diagram
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a methylated C9 triketide
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?
4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA + H2O
2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2
show the reaction diagram
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an unnatural novel diketide
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?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
show the reaction diagram
4-coumaroyl-CoA + methylmalonyl-CoA + H2O
2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2
show the reaction diagram
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one-step decarboxylative condensation of the two substrates
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?
4-coumaroylCoA + 2 malonyl-CoA + H2O
2 CoA + bisnoryangonin + 2 CO2
show the reaction diagram
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
show the reaction diagram
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
?
show the reaction diagram
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-
-
?
anthraniloyl-CoA + malonyl-CoA + H2O
4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
show the reaction diagram
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-
-
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?
anthraniloyl-CoA + methylmalonyl-CoA + H2O
?
show the reaction diagram
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-
-
-
?
caffeoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
show the reaction diagram
caffeoyl-CoA + malonyl-CoA + H2O
?
show the reaction diagram
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-
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?
cinnamoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
show the reaction diagram
cinnamoyl-CoA + malonyl-CoA + H2O
?
show the reaction diagram
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-
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?
D-phenylalanyl-CoA + malonyl-CoA
?
show the reaction diagram
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-
-
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?
D-tryptophanyl-CoA + malonyl-CoA
?
show the reaction diagram
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-
-
-
?
feruloyl-CoA + malonyl-CoA + H2O
2 CoA + (3E)-4-(4-hydroxy-3-methoxyphenyl)but-3-en-2-one + 2 CO2
show the reaction diagram
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?
feruloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
show the reaction diagram
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feruloyl-CoA is the best substrate showing 3fold higher activity than 4-coumaroyl-CoA
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?
L-phenylalanyl-CoA + malonyl-CoA
?
show the reaction diagram
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the enzyme produces a 1:10 mixture of two products from L-phenylalanyl-CoA and malonyl-CoA. The minor product is a tetramic acid monomer, the major product is a tetramic acid dimer
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?
L-tryptophanyl-CoA + malonyl-CoA
?
show the reaction diagram
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?
N-methylanthraniloyl-CoA + (2RS)-methylmalonyl-CoA
4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
show the reaction diagram
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?
N-methylanthraniloyl-CoA + 3 malonyl-CoA + H2O
1,3-dihydroxy-N-methylacridone + ?
show the reaction diagram
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?
N-methylanthraniloyl-CoA + methylmalonyl-CoA + H2O
?
show the reaction diagram
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-
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?
sinapoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
show the reaction diagram
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-
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?
sinapoyl-CoA + malonyl-CoA + H2O
?
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
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.01
4-Coumaroyl-CoA
0.0033
D-phenylalanyl-CoA
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pH 8.0, temperature not specified in the publication
0.0117
L-phenylalanyl-CoA
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pH 8.0, temperature not specified in the publication
0.001 - 0.0233
malonyl-CoA
0.0237
N-methylanthraniloyl-CoA
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pH 8.0, temperature not specified in the publication
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0298
4-Coumaroyl-CoA
Rheum palmatum
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pH 8.0, 30C, recombinant wild-type enzyme
0.135
D-phenylalanyl-CoA
Rheum palmatum
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pH 8.0, temperature not specified in the publication
0.463
L-phenylalanyl-CoA
Rheum palmatum
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pH 8.0, temperature not specified in the publication
0.0296
malonyl-CoA
Rheum palmatum
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pH 8.0, 30C, recombinant wild-type enzyme
0.0247
N-methylanthraniloyl-CoA
Rheum palmatum
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pH 8.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.96
4-Coumaroyl-CoA
Rheum palmatum
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pH 8.0, 30C, recombinant wild-type enzyme
448
1.27
malonyl-CoA
Rheum palmatum
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pH 8.0, 30C, recombinant wild-type enzyme
76
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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maximum for bisnoryangonin formation activity
8 - 8.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 43000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complex between PKS1 and benzalacetone, to 2.0 A resolution, orthorhombic space group P212121, with unit-cell parameters a: 80.23, b: 81.01, c: 122.89 A
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purified enzyme, sitting drop vapour diffusion method, mixing of 500 nl of protein solution containing 20 mg/ml protein in 20 mM HEPES-NaOH, pH 7.5, 100 mM NaCl, and 2 mM DTT, with 500 nl of reservoir solution containing 100 mM MES-NaOH, pH 6.5, 15% w/v PEG 8000, and 200 mM potassium thiocyanate, and equilibration against 0.1 ml of reservoir solution, 3 days, cryoprotection by 20% v/v glycerol in reservoir solution, X-ray diffraction structure determination and analysis at 1.8 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 172fold from fruits by ammonium sulfate fractionation, gel filtration, hydrophobic interaction and anion exchange chromatography, and chromatofocusing
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
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recombinant RiPKS4 from Escherichia coli strain BL21(DE3)pLYsS
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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expression in Escherichia coli
PKS genotyping, gene products RiPKS5, RiPKS6 and RiPKS11 show negligible BAS activity
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RiPKS4, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)pLYsS
sequence comparison
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
rapid induction of the enzyme in cell suspension cultures upon addition of yeast extract
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C197G
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site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme
C197T
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site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme
G256L
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site-directed mutagenesis, the mutant shows 50% reduced activity but an unaltered product pattern compared to the wild-type enzyme
I214L/L215F
L132A
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site-directed mutagenesis, the substitution expands the product chain length to produce 4-coumaroyltriacetic acid lactone after three condensations with malonyl-CoA, but without the formation of the aromatic ring system
L132C
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site-directed mutagenesis, the substitution expands the product chain length to produce 4-coumaroyltriacetic acid lactone after three condensations with malonyl-CoA, but without the formation of the aromatic ring system
L132F
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site-directed mutagenesis, replacement of Leu132 with bulky aromatic residues, Phe, Tyr and Trp, causes a 1.2fold increase in the benzalacetone-forming activity at pH 8.0, whereas the bisnoryangonin-forming activity is retained or significantly decreased at pH 6.5
L132G
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site-directed mutagenesis, no altered activity compared to the wild-type enzyme
L132P
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site-directed mutagenesis, the L132P mutant exhibits drastically decreased benzalacetone- and bisnoryangonin-forming activities
L132S
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site-directed mutagenesis, the substitution expands the product chain length to produce 4-coumaroyltriacetic acid lactone after three condensations with malonyl-CoA, but without the formation of the aromatic ring system
L132T
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site-directed mutagenesis, the chalcone-forming L132T mutant shows broad substrate specificity. It accepts benzoyl-CoA as the starter substrate to produce a trace amount of 2,4,6-trihydroxybenzophenone, after condensations of benzoyl-CoA with three molecules of malonyl-CoA, along with benzoate-primed triketide and tetraketide pyrones as major products
L132T/I214L/L215F
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site-directed mutagenesis, the triple mutation does not improve the chalcone-forming activity, but instead results in a significant loss of activity
L132W
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site-directed mutagenesis, replacement of Leu132 with bulky aromatic residues, Phe, Tyr and Trp, blocks the entrance of the coumaroyl binding pocket and causes a 1.2fold increase in the benzalacetone-forming activity at pH 8.0, whereas the bisnoryangonin-forming activity is retained or significantly decreased at pH 6.5
L132Y
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site-directed mutagenesis, replacement of Leu132 with bulky aromatic residues, Phe, Tyr and Trp, causes a 1.2fold increase in the benzalacetone-forming activity at pH 8.0, whereas the bisnoryangonin-forming activity is retained or significantly decreased at pH 6.5
S338V
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site-directed mutagenesis, the mutant shows 2fold increased activity but an unaltered product pattern compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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possibility of peparation of tetramic acids from various amino acids through the enzyme