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Information on EC 2.3.1.212 - benzalacetone synthase and Organism(s) Rheum palmatum and UniProt Accession Q94FV7
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2.3.1.212 benzalacetone synthaseIUBMB Comments
A polyketide synthase that catalyses the C6-C4 skeleton of phenylbutanoids in higher plants.
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Word Map
- 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
The taxonomic range for the selected organisms is: Rheum palmatum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
benzalacetone synthase, rpbas, hspks3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2
the enzyme shows remarkable substrate tolerance and catalytic versatility, structure-function relationship and functional diversity of type III PKS enzymes, the enzyme catalytic mechanism for the thioester bond cleavage of the enzyme-bound diketide intermediate and the decarboxylation reaction to produce benzalacetone involves Cys164, His33, and Asn336, overview. RpBAS initially accepts the aminoacyl-CoA as a starter, and then recruits malonyl-CoA for a Claisen condensation to generate the gamma-amino-beta-ketothioester. The free gamma-amino group of the enzyme-bound intermediate can cleave the thioester bond, with concomitant intramolecular lactamization
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.
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 + ?
-
-
-
?
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
-
-
-
?
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-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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
D-phenylalanyl-CoA
pH 8.0, temperature not specified in the publication
0.0117
L-phenylalanyl-CoA
pH 8.0, temperature not specified in the publication
0.0237
N-methylanthraniloyl-CoA
pH 8.0, temperature not specified in the publication
0.01
4-coumaroyl-CoA
pH 8.0, 30°C, recombinant wild-type enzyme
additional information
additional information
steady-state enzyme kinetics, overview
-
additional information
additional information
-
steady-state enzyme kinetics, overview
-
additional information
additional information
steady-state enzyme kinetics
-
additional information
additional information
-
steady-state enzyme kinetics
-
additional information
additional information
steady-state kinetics analysis for benzalacetone-, bisnoryangonin-, and chalcone-forming activities, overview
-
additional information
additional information
-
steady-state kinetics analysis for benzalacetone-, bisnoryangonin-, and chalcone-forming activities, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.135
D-phenylalanyl-CoA
pH 8.0, temperature not specified in the publication
0.463
L-phenylalanyl-CoA
pH 8.0, temperature not specified in the publication
0.0247
N-methylanthraniloyl-CoA
pH 8.0, temperature not specified in the publication
0.0298
4-coumaroyl-CoA
pH 8.0, 30°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
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. 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
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
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BAS_RHEPA
384
0
42225
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three-dimensional homology modeling, structure-function relationship , overview
additional information
-
three-dimensional homology modeling, structure-function relationship , overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
I214L/L215F
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
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
possibility of peparation of tetramic acids from various amino acids through the enzyme
synthesis
a de novo pathway for the production of raspberry ketone is assembled using four heterologous genes, encoding phenylalanine/tyrosine ammonia lyase, cinnamate-4-hydroxlase, coumarate-CoA ligase and benzalacetone synthase, in an industrial strain of Saccharomyces cerevisiae. It is possible to produce sensorially-relevant quantities of raspberry ketone in the industrial heterologous host
synthesis
a heterologous pathway to produce raspberry ketone from p-coumaric acid, including 4-coumarate:CoA ligase (4CL), benzalacetone synthase (BAS), and raspberry ketone/zingerone synthase (RZS1) from plants, is assembled in Escherichia coli. Raspberry ketone is an important ingredient in the flavor and fragrance industries. Engineered strain CZ-8 which cooverexpresses At4CL1, RpBAS, and RiRZS1 achieves levels of 90.97 mg/l of raspberry ketone
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
Shimokawa, Y.; Morita, H.; Abe, I.
Benzalacetone synthase
Front. Plant Sci.
3
57
2012
Rheum palmatum (Q94FV7), Rheum palmatum
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
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
Rheum palmatum (Q94FV7)
Abe, I.; Abe, T.; Wanibuchi, K.; Noguchi, H.
Enzymatic formation of quinolone alkaloids by a plant type III polyketide synthase
Org. Lett.
8
6063-6065
2006
Rheum palmatum (Q94FV7), Rheum palmatum
Wang, C.; Zheng, P.; Chen, P.
Construction of synthetic pathways for raspberry ketone production in engineered Escherichia coli
Appl. Microbiol. Biotechnol.
103
3715-3725
2019
Rheum palmatum (Q94FV7)
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