2.3.1.220: 2,4,6-trihydroxybenzophenone synthase
This is an abbreviated version!
For detailed information about 2,4,6-trihydroxybenzophenone synthase, go to the full flat file.
Word Map on EC 2.3.1.220
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2.3.1.220
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falciparum
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plasmodium
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merozoite
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malaria
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subunit-based
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erythrocyte
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aotus
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high-activity
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receptor-ligand
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sporozoite
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anti-malarial
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multi-stage
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protection-inducing
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multiepitope
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hyaluronan
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enzyme-treated
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multi-antigenic
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hyaluronan-binding
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rhoptries
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microneme
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chemically-synthesized
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rhoptry-associated
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parasitophorous
- 2.3.1.220
- falciparum
- plasmodium
-
merozoite
- malaria
-
subunit-based
- erythrocyte
- aotus
-
high-activity
-
receptor-ligand
-
sporozoite
-
anti-malarial
-
multi-stage
-
protection-inducing
-
multiepitope
- hyaluronan
-
enzyme-treated
-
multi-antigenic
-
hyaluronan-binding
-
rhoptries
-
microneme
-
chemically-synthesized
-
rhoptry-associated
-
parasitophorous
Reaction
3 malonyl-CoA + = 4 CoA + + 3 CO2
Synonyms
benzophenone synthase, BPS, HaBPS
ECTree
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General Information
General Information on EC 2.3.1.220 - 2,4,6-trihydroxybenzophenone synthase
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evolution
malfunction
metabolism
additional information
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biphenyl synthase and benzophenone synthase catalyze the formation of identical linear tetraketide intermediates from benzoyl-CoA and three molecules of malonyl-CoA but use alternative intramolecular cyclization reactions to form 3,5-dihydroxybiphenyl and 2,4,6-trihydroxybenzophenone, respectively, phylogenetic analysis, overview. The enzyme belongs to the type iIi polyketide synthase superfamily. The functionally diverse PKSs, which include BIS and BPS, and the ubiquitously distributed chalcone synthases form separate clusters, which originate from a gene duplication event prior to the speciation of the angiosperms
evolution
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BPS is a type III polyketide synthase, PKS, and part of the chalcone synthase group of the superfamily of enzymes
evolution
crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica. The results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants
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the benzophenone synthaase is converted into a functional phenylpyrone synthase by the single amino acid substitution T135L in the initiation/elongation cavity, homology modeling. The intermediate triketide may be redirected into a smaller pocket in the active site cavity, resulting in phenylpyrone formation by lactonization
malfunction
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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
metabolism
the enzyme catalyzes the formation of an intermediate, 2,4,6-trihydroxybenzophenone, in the biosynthetic pathway of alpha-mangostin
the catalytic triad is formed by Cys164, His303, and Asn336
additional information
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residues involved in the initiation pocket are M217, I258, A260, and Y269, and in the elongation pocket T135, S136, T197, M199, T200, S219, M267, and G342, the catalytic triad is formed by residues C167, H307, and N340, molecular modeling constructed based on the crystal structure of Medicago sativa CHS2 complexed with resveratrol, PDB ID 1CGZ, overview
additional information
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the catalytic triad is formed by Cys167, His307, aand Asn340