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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

Reaction

3 malonyl-CoA +

benzoyl-CoA
= 4 CoA +
2,4,6-trihydroxybenzophenone
 + 3 CO2

Synonyms

benzophenone synthase, BPS, HaBPS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.220 2,4,6-trihydroxybenzophenone synthase

Engineering

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

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PROTEIN VARIANTS
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
-
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
-
site-directed mutagenesis, inactive mutant
T135F
-
site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
T135G
-
site-directed mutagenesis, inactive mutant
T135I
-
site-directed mutagenesis, inactive mutant
T135L
-
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
-
site-directed mutagenesis, inactive mutant
T135S
-
site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
T135V
-
site-directed mutagenesis, inactive mutant
T135Y
-
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