Information on EC 2.3.1.220 - 2,4,6-trihydroxybenzophenone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.220
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RECOMMENDED NAME
GeneOntology No.
2,4,6-trihydroxybenzophenone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hyperxanthone E biosynthesis
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tetrahydroxyxanthone biosynthesis (from benzoate)
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benzoyl-CoA degradation
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)
Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3',4,6-tetrahydroxybenzophenone synthase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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 + benzoyl-CoA
3 CoA + 6-phenyl-4-hydroxy-2-pyrone + 2 CO2
show the reaction diagram
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
show the reaction diagram
3 malonyl-CoA + hexanoyl-CoA
4 CoA + 4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + 3 CO2
show the reaction diagram
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-
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?
3 malonyl-CoA + isobutyryl-CoA
4 CoA + phloroisobutyrophenone + 3 CO2
show the reaction diagram
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-
-
-
?
3 malonyl-CoA + isovaleryl-CoA
4 CoA + phloroisovalerophenone + 3 CO2
show the reaction diagram
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-
-
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?
3 malonyl-CoA + phenylacetyl-CoA
4 CoA + 2,4,6-trihydroxyphenylbenzylketone + 3 CO2
show the reaction diagram
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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
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.00965
benzoyl-CoA
0.0087 - 0.0313
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068 - 0.055
benzoyl-CoA
0.0068 - 0.0582
malonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0064 - 5.14
benzoyl-CoA
394
0.0064 - 3.55
malonyl-CoA
76
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.97
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42700
xx * 42700, about, sequence calculation
42800
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2 * 42800
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
xx * 42700, about, sequence calculation
homodimer
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2 * 42800
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reccombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amin acid sequence determination and analysis, sequence comparison and phylogenetic tree
expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A257G
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant A257G gives similar enzyme products as the wild type with both benzoyl-CoA and 4-coumaroyl-CoA
G339S
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant G339S yields high amounts of both benzophenone and triketide lactone type with benzoyl-CoA but shows no activity for 4-coumaroyl-CoA
G339V
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant shows no activity with either benzoyl-CoA or 4-coumaroyl-CoA
T133L
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. With benzoyl-CoA as a starter, the T133L mutant yields triketide lactone as the major enzymatic product
T135L
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the T135L mutant catalyzes the addition of only two acetyl groups to the benzoyl starter unit. The triketide is the final linear intermediate and cyclizes into phenylpyrone via C-5 keto-enol oxygen -> C-1 lactonization. The T135L substitution opens a new pocket, the entrance of which is blocked in the wild-type enzyme by hydrogen bond formation between the threonine side chain and the backbone. Because of the interaction of the lipophilic side chain of the introduced leucine residue with the phenyl group of the growing polyketide chain, the triketide in the active site cavity of the T135L mutant may be redirected into the new pocket
T135A
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site-directed mutagenesis, inactive mutant
T135F
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site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
T135G
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site-directed mutagenesis, inactive mutant
T135I
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site-directed mutagenesis, inactive mutant
T135L
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site-directed mutagenesis, the benzophenone synthaase is converted into a functional phenylpyrone synthase by the single amino acid substitution in the initiation/elongation cavity, chalcone synthase-based homology modeling, overview. The intermediate triketide may be redirected into a smaller pocket in the active site cavity, resulting in phenylpyrone formation by lactonization. Compared with the initiation/elongation cavity of BPS, the size of the newly accessible pocket in PPS is smaller and does not allow for a third acetyl addition to the growing polyketide chain, resulting in the release of the intermediate triketide as 6-phenyl-4-hydroxy-2-pyrone
T135N
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site-directed mutagenesis, inactive mutant
T135S
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site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
T135V
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site-directed mutagenesis, inactive mutant
T135Y
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site-directed mutagenesis, inactive mutant
additional information
homology model of wild-type GmBPS and GmBPS mutants A257G, T133L, G339V, and G339S, active-site architectures by surface models and substrate entrances, overview