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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 + malonyl-CoA + H2O
2 CoA + 4-hydroxybenzalacetone + 2 CO2
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
-
-
?
4-coumaroylCoA + 2 malonyl-CoA + H2O
2 CoA + bisnoryangonin + 2 CO2
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
?
-
-
-
?
anthraniloyl-CoA + malonyl-CoA + H2O
4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
-
-
-
?
anthraniloyl-CoA + methylmalonyl-CoA + H2O
?
-
-
-
?
caffeoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
caffeoyl-CoA + malonyl-CoA + H2O
?
-
-
-
?
cinnamoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
cinnamoyl-CoA + malonyl-CoA + H2O
?
-
-
-
?
D-phenylalanyl-CoA + malonyl-CoA
?
-
-
-
?
D-tryptophanyl-CoA + malonyl-CoA
?
-
-
-
?
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
-
?
L-tryptophanyl-CoA + malonyl-CoA
?
-
-
-
?
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 + ?
-
-
-
?
N-methylanthraniloyl-CoA + methylmalonyl-CoA + H2O
?
-
-
-
?
sinapoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
sinapoyl-CoA + malonyl-CoA + H2O
?
-
-
-
?
additional information
?
-
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
-
-
?
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
5-hydroxyferuloyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
caffeoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
caffeoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
cinnamoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
cinnamoyl-CoA + malonyl-CoA + H2O
2 CoA + ? + 2 CO2
-
-
-
-
?
additional information
?
-
no activity with succinyl-CoA
-
-
?
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
-
-
-
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evolution
-
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily
evolution
-
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily
evolution
-
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily, amino acids C164, F215, H303 and N336 are conserved
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily. BAS lacks the critical residue Phe215, that is important in the polyketide formation reactions, structure-function relationship of the plant type III PKSs, overview. The absence of Phe215 in BAS accounts for the interruption of the polyketide chain elongation at the diketide stage
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily. Comparison of the primary sequences and and secondary structures of BAS and other type III PKSs, overview
evolution
the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily. Members of the CHS-superfamily enzymes do not form a species-specific cluster, but instead group into subfamilies according to their enzymatic function. BAS lacks the active-site Phe215 residue (numbering in CHS), which has been proposed to help orient substrates and intermediates during the sequential condensation of 4-coumaroyl-CoA with malonyl-CoA in CHS, while the catalytic cysteine-histidine dyad (Cys164-His303) in CHS is well conserved in BAS
physiological function
-
4-hydroxybenzalacetone, i.e. 4-hydroxyphenylbutan-2-one, the characteristic aroma compound of raspberries, is synthesized from 4-coumaryl-CoA and malonyl-CoA in a two-step reaction sequence that is catalyzed by benzalacetone synthase and benzalacetone reductase. 4-Hydroxybenzalacetone inhibits mycelial growth of the raspberry pathogen Phytophthora fragariae var. rub
physiological function
BAS plays a crucial role in the biosynthesis of pharmaceutically important phenylbutanone glucoside, lindleyin, the active principle of the anti-inflammatory action of the medicinal plant, and it plays a crucial role for the construction of the C6-C4 moiety of a variety of natural products such as medicinally important gingerols in ginger plant
physiological function
benzalacetone synthase from Rheum palmatum efficiently catalyzes condensation of N-methylanthraniloyl-CoA (or anthraniloyl-CoA) with malonyl-CoA (or methylmalonyl-CoA) to produce 4-hydroxy-2(1H)-quinolones, a novel alkaloidal scaffold produced by a type III polyketide synthase, PKS. The quinolone alkaloids act as N-methyl-D-aspartate and serotonin 5-HT3 receptor antagonists. Moreover, they are also important intermediates in the chemical synthesis of alkaloids
physiological function
pBAS catalyzes the one-step, decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the C6-C4 benzalacetone scaffold
physiological function
-
the enzyme is a polyketide synthase, PKS, involved in the raspberry flavor and color polyketide-derivatives biosynthetic pathway, developmental regulation of PKS during fruit ripening, overview
physiological function
-
4-hydroxybenzalacetone, i.e. 4-hydroxyphenylbutan-2-one, the characteristic aroma compound of raspberries, is synthesized from 4-coumaryl-CoA and malonyl-CoA in a two-step reaction sequence that is catalyzed by benzalacetone synthase and benzalacetone reductase. 4-Hydroxybenzalacetone inhibits mycelial growth of the raspberry pathogen Phytophthora fragariae var. rub
-
additional information
pH-dependence of benzalacetone and bisnoryangonin production. Residues Ile214 and Leu215 are responsible for the diketide formation activity, unlike the case of CHS with residues L214 and F215, BAS utilizes an alternative pocket to lock the coumaroyl moiety for the diketide formation reaction, the second active-site Cys is not involved in the enzyme reaction,and Cys197 is not essential for the 4-hydroxybenzalacetone-producing activity, homology modeling
additional information
-
pH-dependence of benzalacetone and bisnoryangonin production. Residues Ile214 and Leu215 are responsible for the diketide formation activity, unlike the case of CHS with residues L214 and F215, BAS utilizes an alternative pocket to lock the coumaroyl moiety for the diketide formation reaction, the second active-site Cys is not involved in the enzyme reaction,and Cys197 is not essential for the 4-hydroxybenzalacetone-producing activity, homology modeling
additional information
structure-function relationship, homology modeling, overview
additional information
-
structure-function relationship, homology modeling, overview
additional information
structure-function relationship, overview
additional information
-
structure-function relationship, overview
additional information
the absence of Phe215 in BAS accounts for the interruption of the polyketide chain elongation at the diketide stage compared to chalcone synthase, EC 2.3.1.74, structure-function relationship , overview. BAS catalytic residues are Asn336, His303, and Cys164, active site structure, overview
additional information
-
the absence of Phe215 in BAS accounts for the interruption of the polyketide chain elongation at the diketide stage compared to chalcone synthase, EC 2.3.1.74, structure-function relationship , overview. BAS catalytic residues are Asn336, His303, and Cys164, active site structure, overview
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C197G
site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme
C197T
site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme
G256L
site-directed mutagenesis, the mutant shows 50% reduced activity but an unaltered product pattern compared to the wild-type enzyme
L132A
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
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
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
site-directed mutagenesis, no altered activity compared to the wild-type enzyme
L132P
site-directed mutagenesis, the L132P mutant exhibits drastically decreased benzalacetone- and bisnoryangonin-forming activities
L132S
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
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
site-directed mutagenesis, the triple mutation does not improve the chalcone-forming activity, but instead results in a significant loss of activity
L132W
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
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
site-directed mutagenesis, the mutant shows 2fold increased activity but an unaltered product pattern compared to the wild-type enzyme
I214L/L215F
site-directed mutagenesis, the mutant restores chalcone-forming activity
I214L/L215F
site-directed mutagenesis, the mutation restores the active site residues of chalcone synthase, the mutant shows chalcone-forming activity, EC 2.3.1.74. The mutant enzyme thus exhibits 36fold decreases in kcat/Km for 4-coumaroyl-CoA and 20fold decreases in kcat/Km for malonyl-CoA compared with wild-type BAS, kinetics of chalcone naringenin-forming activity at pH 6.5, overview
additional information
formation of other products such as a tetraketide pyrone 4-coumaroyltriacetic acid lactone or naringenin chalcone is not detected for all the mutant enzymes
additional information
-
formation of other products such as a tetraketide pyrone 4-coumaroyltriacetic acid lactone or naringenin chalcone is not detected for all the mutant enzymes
additional information
the single amino acid substitution L132T restores the chalcone-forming activity of chalcone synthase, EC 2.3.1.74, in BAS, probably due to restoration of the coumaroyl binding pocket in the active-site cavity, whereas the Ala, Ser, and Cys substitutions expand 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
additional information
-
the single amino acid substitution L132T restores the chalcone-forming activity of chalcone synthase, EC 2.3.1.74, in BAS, probably due to restoration of the coumaroyl binding pocket in the active-site cavity, whereas the Ala, Ser, and Cys substitutions expand 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
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Zheng, D.; Hrazdina, G.
Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.)
Arch. Biochem. Biophys.
470
139-145
2008
Rubus idaeus (B0LDU5)
brenda
Morita, H.; Shimokawa, Y.; Tanio, M.; Kato, R.; Noguchi, H.; Sugio, S.; Kohno, T.; Abe, I.
A structure-based mechanism for benzalacetone synthase from Rheum palmatum
Proc. Natl. Acad. Sci. USA
107
669-673
2010
Rheum palmatum
brenda
Morita, H.; Tanio, M.; Kondo, S.; Kato, R.; Wanibuchi, K.; Noguchi, H.; Sugio, S.; Abe, I.; Kohno, T.
Crystallization and preliminary crystallographic analysis of a plant type III polyketide synthase that produces benzalacetone
Acta Crystallogr. Sect. F
64
304-306
2008
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Abe, T.; Morita, H.; Noma, H.; Kohno, T.; Noguchi, H.; Abe, I.
Structure function analysis of benzalacetone synthase from Rheum palmatum
Bioorg. Med. Chem. Lett.
17
3161-3166
2007
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Shimokawa, Y.; Morita, H.; Abe, I.
Structure-based engineering of benzalacetone synthase
Bioorg. Med. Chem. Lett.
20
5099-5103
2010
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Abe, I.; Takahashi, Y.; Morita, H.; Noguchi, H.
Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum
Eur. J. Biochem.
268
3354-3359
2001
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Shimokawa, Y.; Morita, H.; Abe, I.
Benzalacetone synthase
Front. Plant Sci.
3
57
2012
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Abe, I.; Sano, Y.; Takahashi, Y.; Noguchi, H.
Site-directed mutagenesis of benzalacetone synthase. The role of the Phe215 in plant type III polyketide synthases
J. Biol. Chem.
278
25218-25226
2003
Rheum palmatum (Q94FV7), Rheum palmatum
brenda
Abe, I.; Takahashi, Y.; Noguchi, H.
Enzymatic formation of an unnatural C6-C5 aromatic polyketide by plant type III polyketide synthases
Org. Lett.
4
3623-3626
2002
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Rheum palmatum (Q94FV7)
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Polygonum cuspidatum
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