2.3.1.212: benzalacetone synthase
This is an abbreviated version!
For detailed information about benzalacetone synthase, go to the full flat file.
Word Map on EC 2.3.1.212
-
2.3.1.212
-
polyketide
-
chalcone
-
palmatum
-
rheum
-
plant-specific
-
raspberry
-
diketide
-
phenylbutanoids
-
flavor
-
unnatural
-
p-coumaric
-
4-coumarate
-
synthesis
-
stilbene
-
phenylpropanoids
-
crispum
-
idaeus
-
methylmalonyl-coa
-
cuspidatum
-
condensations
-
naringenin
-
arachis
-
polygonum
-
petroselinum
-
baicalensis
-
fragrance
-
rhubarb
-
scutellaria
-
tetraketide
-
quinolone
-
rubus
-
p-coumaroyl-coa
- 2.3.1.212
- polyketide
- chalcone
- palmatum
- rheum
-
plant-specific
- raspberry
-
diketide
-
phenylbutanoids
-
flavor
-
unnatural
-
p-coumaric
- 4-coumarate
- synthesis
- stilbene
-
phenylpropanoids
- crispum
- idaeus
- methylmalonyl-coa
- cuspidatum
-
condensations
- naringenin
- arachis
-
polygonum
-
petroselinum
- baicalensis
-
fragrance
- rhubarb
-
scutellaria
-
tetraketide
-
quinolone
-
rubus
- p-coumaroyl-coa
Reaction
Synonyms
bAS, HsPKS3, PKS1, RinPKS1, RiPKS4, RpBAS
ECTree
2.3.1.212 benzalacetone synthaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.1.212 - benzalacetone synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
3 (2RS)-methylmalonyl-CoA + H2O
6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone + ?
-
a methylated C9 triketide
-
?
4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA + H2O
2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2
-
an unnatural novel diketide
-
?
4-coumaroyl-CoA + methylmalonyl-CoA + H2O
2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2
one-step decarboxylative condensation of the two substrates
-
-
?
anthraniloyl-CoA + malonyl-CoA + H2O
4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
-
-
-
?
feruloyl-CoA + malonyl-CoA + H2O
2 CoA + (3E)-4-(4-hydroxy-3-methoxyphenyl)but-3-en-2-one + 2 CO2
-
-
-
?
feruloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
feruloyl-CoA is the best substrate showing 3fold higher activity than 4-coumaroyl-CoA
-
-
?
feruloyl-CoA + malonyl-CoA + H2O
?
77% activity compared to 4-coumaroyl-CoA
-
-
?
L-phenylalanyl-CoA + malonyl-CoA
?
-
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
-
?
N-methylanthraniloyl-CoA + (2RS)-methylmalonyl-CoA
4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
-
-
-
?
N-methylanthraniloyl-CoA + 3 malonyl-CoA + H2O
1,3-dihydroxy-N-methylacridone + ?
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
the enzyme catalyzes the formation of unnatural 2-substituted quinolones and 1,3-diketones via head-to-head condensation of two completely different substrates. The broad range of substrate tolerance of HsPKS3 facilitates accessing structurally diverse 2-substituted quinolones and 1,3-diketones
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
a one-step decarboxylative condensation at pH 8.0
i.e. 4-(4-hydroxyphenyl)but-3-en-2-one
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
BAS catalyzes the decarboxylative coupling of 4-coumaroyl-CoA with malonyl-CoA to produce the diketide benzalacetone
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
one-step condensation
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
one-step decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the diketide 4-(4-hydroxyphenyl)-but-3-en-2-one
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
high activity with 4-coumaroyl-CoA
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
the enzyme effectively yields 4-hydroxybenzalacetone as a dominant product at pH 9.5
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
when incubated with 4-coumaroyl-CoA and malonyl-CoA as substrates at pH 7.5, the enzyme catalyzes the formation of naringenin chalcone as a major product, along with 4-hydroxybenzalacetone. At pH 9.5, the enzyme effectively yields 4-hydroxybenzalacetone as a dominant product, along with naringenin chalcone
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
high activity with 4-coumaroyl-CoA
-
-
?
4-coumaroylCoA + 2 malonyl-CoA + H2O
2 CoA + bisnoryangonin + 2 CO2
-
-
-
?
4-coumaroylCoA + 2 malonyl-CoA + H2O
2 CoA + bisnoryangonin + 2 CO2
wild-type and mutant BAS all afford the triketide pyrone bisnoryangonin after two condensations with malonyl-CoA at acidic pH 6.0
-
-
?
additional information
?
-
RpBAS also accepts a series of aminoacyl-CoA thioesters as starter substrates, and catalyzes their condensation with one molecule of malonyl-CoA to produce the tetramic acid (2,4-pyrrolidinedione)derivatives. RpBAS also accepts (2RS)-methylmalonyl-CoA as the only substrate to produce a methylated C9 triketide, 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone, as a single product from three molecules of (2RS)-methylmalonyl-CoA. Substrate specificity, overview
-
-
?
additional information
?
-
-
RpBAS also accepts a series of aminoacyl-CoA thioesters as starter substrates, and catalyzes their condensation with one molecule of malonyl-CoA to produce the tetramic acid (2,4-pyrrolidinedione)derivatives. RpBAS also accepts (2RS)-methylmalonyl-CoA as the only substrate to produce a methylated C9 triketide, 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone, as a single product from three molecules of (2RS)-methylmalonyl-CoA. Substrate specificity, overview
-
-
?
additional information
?
-
the enzyme reaction with the anthraniloyl-CoA proceeds without the decarboxylation step, and the amide formation immediately follows the condensation reactions of N-methylanthraniloyl-CoA (or anthraniloyl-CoA) and malonyl-CoA (or methylmalonyl-CoA), mechanism, overview
-
-
?
additional information
?
-
-
the enzyme reaction with the anthraniloyl-CoA proceeds without the decarboxylation step, and the amide formation immediately follows the condensation reactions of N-methylanthraniloyl-CoA (or anthraniloyl-CoA) and malonyl-CoA (or methylmalonyl-CoA), mechanism, overview
-
-
?
additional information
?
-
the recombinant enzyme expressed in Escherichia coli efficiently affords benzalacetone as a single product from 4-coumaroyl-CoA and malonyl-CoA. BAS does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. No conversion of 3-(4-hydroxyphenyl)propionyl-CoA to 4-(4-hydroxyphenyl)butan-2-one
-
-
?
additional information
?
-
-
the recombinant enzyme expressed in Escherichia coli efficiently affords benzalacetone as a single product from 4-coumaroyl-CoA and malonyl-CoA. BAS does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. No conversion of 3-(4-hydroxyphenyl)propionyl-CoA to 4-(4-hydroxyphenyl)butan-2-one
-
-
?
additional information
?
-
the wild-type enzyme also shows formation of benzalacetone, bisnoryangonin, and naringenin chalcone from 4-coumaroyl-CoA and malonyl-CoA as substrates, cf. EC 2.3.1.74, as well as formation of triacetic acid lactone, 5,7-dihydroxy-2-methylchromone, and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one (SEK4) and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one (SEK4b), from malonyl-CoA as a substrate, mechanisms, overview
-
-
?
additional information
?
-
-
the wild-type enzyme also shows formation of benzalacetone, bisnoryangonin, and naringenin chalcone from 4-coumaroyl-CoA and malonyl-CoA as substrates, cf. EC 2.3.1.74, as well as formation of triacetic acid lactone, 5,7-dihydroxy-2-methylchromone, and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one (SEK4) and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one (SEK4b), from malonyl-CoA as a substrate, mechanisms, overview
-
-
?
additional information
?
-
RiPKS4 is a bifunctional polyketide synthase producing both 4-hydroxybenzalacetone and naringenin chalcone, the latter by reaction of chalcone synthase, EC 2.3.1.74. The recombinant RiPKS4 protein, like the native protein from raspberry fruits accepts 4-coumaryl-CoA and ferulyl-CoA as starter substrates and catalyzes the formation of both naringenin chalcone, 4-hydroxy-benzalacetone, and 3-methoxy-4-hydroxy-benzalacetone. The activity of RiPKS4 is higher with ferulyl-CoA than with 4-coumaryl-CoA
-
-
?
additional information
?
-
4-coumaroyl-CoA and feruloyl-CoA are the only cinnamoyl-CoA derivatives accepted as starter substrates. RinPKS1 does not accept isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
-
-
-
additional information
?
-
the enzyme does not accept cinnamoyl-CoA, caffeoyl-CoA, benzoyl-CoA, isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
-
-
-
