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Information on EC 2.3.1.151 - 2,3',4,6-tetrahydroxybenzophenone synthase
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EC Tree
2.3.1.151 2,3',4,6-tetrahydroxybenzophenone synthaseIUBMB Comments
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).
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Word Map
- 2.3.1.151
- xanthones
- polyketide
- chalcone
- malonyl-coas
-
hypericum
- synthases
- androsaemum
-
benzoic
- 4-coumaroyl-coa
- biphenyls
-
starter
- mangostana
- perforatum
-
cinnamic
-
garcinia
-
phytoalexins
- dibenzofurans
- rosaceae
-
polyprenylated
-
sorbus
- clusiaceae
- aucuparia
-
centaurium
-
triketide
- erythraea
-
acid-specific
-
ammonia-lyase
- maloideae
- pericarps
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
benzophenone synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3',4,6-Tetrahydroxybenzophenone synthase
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-
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benzophenone synthase
BPS
Synthase, benzophenone
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-
-
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additional information
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enzyme belongs to the plant polyketid synthase superfamily, i.e. type III PKSs
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 Malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
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-
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3 Malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
reaction mechanism, multiple decarboxylative condensation with malonyl-CoA followed by cyclization and aromatization of the inter,ediate tetraketide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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decarboxylation
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intramolecular cyclization
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PATHWAY SOURCE
PATHWAYS
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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).
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CAS REGISTRY NUMBER
COMMENTARY
175780-21-9
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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
2 malonyl-CoA + 4-coumaroyl-CoA
3 CoA + 4-hydroxy-6-[(E)-2-(4-hydroxyphenyl)ethenyl]-2H-pyran-2-one + 2 CO2
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-
-
?
3 malonyl-CoA + acetyl-CoA
4 CoA + 4-hydroxy-6-methyl-2H-pyran-2-one + 3 CO2
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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
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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 + benzoyl-CoA
4 CoA + 6-phenyl-4-hydroxy-2-pyrone + 3 CO2
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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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-
?
3 malonyl-CoA + cinnamoyl-CoA
4 CoA + 4-hydroxy-6-[(E)-2-phenylethenyl]-2H-pyran-2-one + 3 CO2
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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
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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
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-
-
?
3 malonyl-CoA + salicyl-CoA
4 CoA + 4-hydroxy-2H-chromen-2-one + 3 CO2
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-
?
3-hydroxybenzoyl-CoA + 3 malonyl-CoA
2,3',4,6-tetrahydroxybenzophenone + 4 CoA + 3 CO2
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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
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-
?
4-hydroxybenzoyl-CoA + 3 malonyl-CoA
2,4,4',6-trihydroxybenzophenone + 4 CoA + 3 CO2
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very low activity, stepwise condensation
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?
Malonyl-CoA + 3-hydroxybenzoyl-CoA
?
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central step in xanthone biosynthesis
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?
Malonyl-CoA + 4-hydroxybenzoyl-CoA
?
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5% of the activity with benzoyl-CoA
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?
N-methylanthraniloyl-CoA + malonyl-CoA
? + CoA + CO2
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low activity, stepwise condensation
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?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 2,4,6-trihydroxybenzophenone + 2 CO2
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44% of the activity with 3-hydroxybenzoyl-CoA
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?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 2,4,6-trihydroxybenzophenone + 2 CO2
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?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 2,4,6-trihydroxybenzophenone + 2 CO2
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enzyme is inactive with CoA-linked cinnamic acids
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?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 2,4,6-trihydroxybenzophenone + 2 CO2
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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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-
?
3 malonyl-CoA + 3-hydroxybenzoyl-CoA
4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
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?
3 malonyl-CoA + 3-hydroxybenzoyl-CoA
4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
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3-hydroxybenzoyl-CoA is the preferred substrate
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-
?
3 malonyl-CoA + 3-hydroxybenzoyl-CoA
4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
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49% of the activity with benzyol-CoA
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?
3 malonyl-CoA + 3-hydroxybenzoyl-CoA
4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
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relative activity: 57%
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?
benzoyl-CoA + 3 malonyl-CoA
2,4,6-trihydroxybenzophenone + 4 CoA + 3 CO2
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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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?
benzoyl-CoA + 3 malonyl-CoA
2,4,6-trihydroxybenzophenone + 4 CoA + 3 CO2
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preferred substrate, stepwise condensation
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?
additional information
?
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with acetyl CoA or malonyl CoA as a starter substrate, the enzyme only produces a triacetic lactone of triketide lactone type, with phenylacetyl-Coa also lactones of tetraketide and triketide type, and with hexanoyl-CoA phloroglucinol and triketide type lactones, substrate specificity, overview
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?
additional information
?
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with acetyl CoA or malonyl CoA as a starter substrate, the enzyme only produces a triacetic lactone of triketide lactone type, with phenylacetyl-Coa also lactones of tetraketide and triketide type, and with hexanoyl-CoA phloroglucinol and triketide type lactones, substrate specificity, overview
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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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?
additional information
?
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no activity with activated cinnamic acids as starter compounds, e.g. 2-hydroxybenzoyl-CoA, 4-coumaroyl-CoA, 3-coumaroyl-CoA, 2-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA, and feruloyl-CoA, no activity with acetyl-CoA, substrate specificity, overview
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?
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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
benzoyl-CoA + 3 malonyl-CoA
2,4,6-trihydroxybenzophenone + 4 CoA + 3 CO2
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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
?
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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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-
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
required for maximum activity, without DTT the enzyme shows 40% of maximal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
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pH 6.0: about 20% of maximal activity, pH 8.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
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about 55% of maximal activity, 5°C: about 30% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of GmBPS in fruit pericarp from an early stage
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
additional information
the catalytic triad is formed by Cys164, His303, and Asn336
additional information
-
the catalytic triad is formed by Cys164, His303, and Asn336
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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). TBSYN_HYPAN
395
0
42828
Swiss-Prot
other Location (Reliability: 2)
K4HQC0_9ROSI
395
0
42711
TrEMBL
other Location (Reliability: 2)
A0A2H4KKK6_HYPPE
395
0
43192
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42800
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
2 * 44000, His-tagged enzyme, SDS-PAGE; 2 * 45618, His-tagged enzyme, sequence calculation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
T135F
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mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities
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
T135S
-
mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities
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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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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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beerhues, L.
Benzophenone synthase from cultured cells of Centaurium erythraea
FEBS Lett.
383
264-266
1996
Centaurium erythraea
brenda
Schmidt, W.; Beerhues, L.
Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum
FEBS Lett.
420
143-146
1997
Hypericum androsaemum
brenda
Liu, B.; Falkenstein-Paul, H.; Schmidt, W.; Beerhues, L.
Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases
Plant J.
34
847-855
2003
Hypericum androsaemum
brenda
Klingauf, P.; Beuerle, T.; Mellenthin, A.; El-Moghazy, S.A.; Boubakir, Z.; Beerhues, L.
Biosynthesis of the hyperforin skeleton in Hypericum calycinum cell cultures
Phytochemistry
66
139-145
2005
Hypericum calycinum
brenda
Klundt, T.; Bocola, M.; Luetge, M.; Beuerle, T.; Liu, B.; Beerhues, L.
A single amino acid substitution converts benzophenone synthase into phenylpyrone synthase
J. Biol. Chem.
284
30957-30964
2009
Hypericum androsaemum
brenda
Beerhues, L.; Liu, B.
Biosynthesis of biphenyls and benzophenones-evolution of benzoic acid-specific type III polyketide synthases in plants
Phytochemistry
70
1719-1727
2009
Centaurium erythraea, Hypericum androsaemum
brenda
Nualkaew, N.; Morita, H.; Shimokawa, Y.; Kinjo, K.; Kushiro, T.; De-Eknamkul, W.; Ebizuka, Y.; Abe, I.
Benzophenone synthase from Garcinia mangostana L. pericarps
Phytochemistry
77
60-69
2012
Garcinia mangostana (L7NCQ3), Garcinia mangostana
brenda
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