Information on EC 2.3.1.151 - 2,3',4,6-tetrahydroxybenzophenone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.151
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RECOMMENDED NAME
GeneOntology No.
2,3',4,6-tetrahydroxybenzophenone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 Malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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Claisen condensation
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condensation
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decarboxylation
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intramolecular cyclization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrahydroxyxanthone biosynthesis (from 3-hydroxybenzoate)
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:3-hydroxybenzoyl-CoA malonyltransferase (decarboxylating, 2,3',4,6-tetrahydroxybenzophenone-forming)
Involved in the biosynthesis of plant xanthones. Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA (cf. EC 2.3.1.220, 2,4,6-trihydroxybenzophenone synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
175780-21-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Garcinia mangostana BPS is an enzyme in the family of type III polyketide synthases and shows an amino acid sequence identity of 77-78% with other plant BPSs belonging to the same family (Clusiaceae). The three BPSs from the xanthone-rich Clusiaceae plants, Garcinia mangostana, Hypericum androsaemum, and Hypericum perforatum, suggest a close evolutionary relationship among these enzymes
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
2 malonyl-CoA + 4-coumaroyl-CoA
3 CoA + 4-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-2H-pyran-2-one + 2 CO2
show the reaction diagram
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-
-
?
3 malonyl-CoA + acetyl-CoA
4 CoA + 4-hydroxy-6-methyl-2H-pyran-2-one + 3 CO2
show the reaction diagram
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-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 4-hydroxy-6-(2-oxo-2-phenylethyl)-2H-pyran-2-one + 4-hydroxy-6-phenyl-2H-pyran-2-one + 3 CO2
show the reaction diagram
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the recombinant enzyme produces 2,4,6-trihydroxybenzophenone as the predominant product with benzoyl CoA as substrate but also lactones of tetraketide and triketide type
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?
3 malonyl-CoA + cinnamoyl-CoA
4 CoA + 4-hydroxy-6-[(E)-2-phenylethenyl]-2H-pyran-2-one + 3 CO2
show the reaction diagram
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-
-
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + 4-hydroxy-6-pentyl-2H-pyran-2-one + 5-hexanoyl-4-hydroxy-6-methyl-2H-pyran-2-one + 3 CO2
show the reaction diagram
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-
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?
3 malonyl-CoA + phenylacetyl-CoA
4 CoA + 4-hydroxy-6-(2-oxo-3-phenylpropyl)-2H-pyran-2-one + 6-benzyl-4-hydroxy-2H-pyran-2-one + 2-phenyl-1-(2,4,6-trihydroxyphenyl)ethanone + 3 CO2
show the reaction diagram
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-
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?
3 malonyl-CoA + salicyl-CoA
4 CoA + 4-hydroxy-2H-chromen-2-one + 3 CO2
show the reaction diagram
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-
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?
3-hydroxybenzoyl-CoA + malonyl-CoA
2,4,6-trihydroxybenzophenone + CoA + CO2
show the reaction diagram
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low activity, stepwise condensation
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?
4 malonyl-CoA
4 CoA + 4-hydroxy-6-methyl-2H-pyran-2-one + 3 CO2
show the reaction diagram
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?
4-hydroxybenzoyl-CoA + malonyl-CoA
2,4,6-trihydroxybenzophenone + CoA + CO2
show the reaction diagram
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very low activity, stepwise condensation
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?
benzoyl-CoA + malonyl-CoA
2,4,6-trihydroxybenzophenone + CoA + CO2
show the reaction diagram
Malonyl-CoA + 3-hydroxybenzoyl-CoA
?
show the reaction diagram
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central step in xanthone biosynthesis
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malonyl-CoA + 3-hydroxybenzoyl-CoA
CoA + 2,3',4,5-tetrahydroxybenzophenone + CO2
show the reaction diagram
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relative activity: 57%
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?
malonyl-CoA + 3-hydroxybenzoyl-CoA
CoA + 2,3',4,6-tetrahydroxybenzophenone + CO2
show the reaction diagram
Malonyl-CoA + 4-hydroxybenzoyl-CoA
?
show the reaction diagram
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5% of the activity with benzoyl-CoA
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Malonyl-CoA + benzoyl-CoA
CoA + 2,4,6-trihydroxybenzophenone + CO2
show the reaction diagram
malonyl-CoA + benzoyl-CoA
CoA + 6-phenyl-4-hydroxy-2-pyrone + CO2
show the reaction diagram
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relative activity: 100%, wildtype benzophenone synthase forms 2,4,6-trihydroxybenzophenone as a major product when incubated with benzoyl-CoA and malonyl-CoA, along with small amounts of 6-phenyl-4-hydroxy-2-pyrone
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?
N-methylanthraniloyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
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low activity, stepwise condensation
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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
benzoyl-CoA + malonyl-CoA
2,4,6-trihydroxybenzophenone + CoA + CO2
show the reaction diagram
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stepwise condensation, polyketid synthesis, benzoic acid biosynthetic pathway overview, the 3'-hydroxylation is catalyzed by a cytochrome P450 monooxygenase in Hypericum androsaemum
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?
Malonyl-CoA + 3-hydroxybenzoyl-CoA
?
show the reaction diagram
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central step in xanthone biosynthesis
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additional information
?
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benzoyl-CoA is a minor starter molecule of polyketid synthesis for PKS in other plants, phylogenetic analysis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
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required for maximum activity, without DTT the enzyme shows 40% of maximal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.00963
benzoyl-CoA
0.0087 - 0.031
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00685 - 9.66
benzoyl-CoA
0.058
malonyl-CoA
Garcinia mangostana
L7NCQ3
pH 7.0, 30C, recombinant His-tagged BPS
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.414 - 6.833
benzoyl-CoA
394
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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pH 6.0: about 20% of maximal activity, pH 8.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
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about 55% of maximal activity, 5C: about 30% of maximal activity
35 - 40
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optimal temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.97
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of GmBPS in fruit pericarp from an early stage
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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SDS-PAGE, molecular weight of mutant T135L
44000
2 * 44000, His-tagged enzyme, SDS-PAGE; 2 * 45618, His-tagged enzyme, sequence calculation
45618
2 * 44000, His-tagged enzyme, SDS-PAGE; 2 * 45618, His-tagged enzyme, sequence calculation
88000
His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, phylogenetic analysis, recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3), GST-tag is cleaved of by factor Xa
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purified on a nickel-nitrilotriacetic acid affinity matrix
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recombinant C-terminally His-tagged BPS from Escherichia coli
separation of benzophenone synthase, isobutyrophenone synthase, and chalcone synthase activities
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of cDNA library, DNA and amino acid sequence determination and analysis, functional overexpression of wild-type enzyme and expression of mutant enzymes in Escherichia coli strain BL21(DE3) as GST fusion protein
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DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression of C-terminally His-tagged BPS in Escherichia coli
expressed in Escherichia coli
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two cDNAs are isolated and heterologously expressed but both enzymes are inactive
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wild-type benzophenone synthase and enzyme mutants are heterologously expressed as N-terminally His6-tagged proteins in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A257G
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme
G339S
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme
G339V
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme
T133L
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme
T135A
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inactive enzyme
T135F
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mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities
T135G
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inactive enzyme
T135I
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inactive enzyme
T135L
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a point mutation in the active site cavity transforms benzophenone synthase into a functional phenylpyrone synthase (PPS). The dramatic change in both substrate and product specificities of benzophenone synthase is rationalized by homology modeling. The mutation may open a new pocket that accommodates the phenyl moiety of the triketide intermediate but limits polyketide elongation to two reactions, resulting in phenylpyrone formation. kcat (substrate: benzoyl-CoA): 0.0086/sec, Km (benzoyl-CoA): 0.001 mM, Km (malonyl-CoA): 8.7 mM. In contrast to the wild-type enzyme, the T135L mutant forms phenylpyrone as a major product and only traces of 2,4,6-trihydroxybenzophenone when incubated with benzoyl-CoA and malonyl-CoA. T135L mutant is almost inactive with 3-hydroxybenzoyl-CoA
T135N
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inactive enzyme
T135S
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mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities
T135V
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inactive enzyme
T135Y
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inactive enzyme