2.3.1.151: 2,3',4,6-tetrahydroxybenzophenone synthase
This is an abbreviated version!
For detailed information about 2,3',4,6-tetrahydroxybenzophenone synthase, go to the full flat file.
Word Map on EC 2.3.1.151
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2.3.1.151
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xanthones
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polyketide
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chalcone
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malonyl-coas
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hypericum
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synthases
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androsaemum
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benzoic
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4-coumaroyl-coa
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biphenyls
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starter
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mangostana
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perforatum
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cinnamic
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garcinia
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phytoalexins
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dibenzofurans
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rosaceae
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polyprenylated
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sorbus
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clusiaceae
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aucuparia
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centaurium
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triketide
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erythraea
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acid-specific
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ammonia-lyase
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maloideae
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pericarps
- 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
Reaction
3 Malonyl-CoA + = 4 CoA + + 3 CO2
Synonyms
2,3',4,6-Tetrahydroxybenzophenone synthase, benzophenone synthase, BPS, More, Synthase, benzophenone
ECTree
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Engineering
Engineering on EC 2.3.1.151 - 2,3',4,6-tetrahydroxybenzophenone synthase
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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
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mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities