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Literature summary extracted from

  • Beerhues, L.; Liu, B.
    Biosynthesis of biphenyls and benzophenones-evolution of benzoic acid-specific type III polyketide synthases in plants (2009), Phytochemistry, 70, 1719-1727.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.151 expressed in Escherichia coli Hypericum androsaemum
2.3.1.151 two cDNAs are isolated and heterologously expressed but both enzymes are inactive Centaurium erythraea

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.208 S338G CHS numbering, site-directed mutagenesis of the mechanistically important residue Sorbus aucuparia
2.3.1.208 T132A CHS numbering, site-directed mutagenesis of the mechanistically important residue Sorbus aucuparia
2.3.1.220 T135A site-directed mutagenesis, inactive mutant Sorbus aucuparia
2.3.1.220 T135F site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme Sorbus aucuparia
2.3.1.220 T135G site-directed mutagenesis, inactive mutant Sorbus aucuparia
2.3.1.220 T135I site-directed mutagenesis, inactive mutant Sorbus aucuparia
2.3.1.220 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 Sorbus aucuparia
2.3.1.220 T135N site-directed mutagenesis, inactive mutant Sorbus aucuparia
2.3.1.220 T135S site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme Sorbus aucuparia
2.3.1.220 T135V site-directed mutagenesis, inactive mutant Sorbus aucuparia
2.3.1.220 T135Y site-directed mutagenesis, inactive mutant Sorbus aucuparia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.151 0.0086
-
 benzoyl-CoA
-
 Hypericum androsaemum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.151 42800
-
-
 Hypericum androsaemum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.208 malonyl-CoA + 2-hydroxybenzoyl-CoA Sorbus aucuparia
-
 2 CoA + 4-hydroxycoumarin + CO2
-
 ?
2.3.1.208 additional information Sorbus aucuparia bifunctional enzyme, biphenyl synthase, BIS, catalyzes the formation of a linear tetraketide intermediate from benzoyl-CoA and three molecules of malonyl-CoA but uses an alternative intramolecular cyclization reaction to form 3,5-dihydroxybiphenyl, EC 2.3.1.177. When incubated with 2-hydroxybenzoyl (salicyl)-CoA, BIS catalyzes a single decarboxylative condensation with malonyl-CoA to form 4-hydroxycoumarin, EC 2.3.1.208 ?
-
 ?
2.3.1.220 3 malonyl-CoA + benzoyl-CoA Sorbus aucuparia
-
 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.151 Centaurium erythraea
-
-
-
2.3.1.151 Hypericum androsaemum
-
-
-
2.3.1.177 Sorbus aucuparia
-
-
-
2.3.1.208 Sorbus aucuparia
-
-
-
2.3.1.220 Sorbus aucuparia
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.151 cell culture
-
 Centaurium erythraea
-
2.3.1.208 cell culture elicitor-treated Sorbus aucuparia
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.151 2 malonyl-CoA + benzoyl-CoA enzyme is inactive with CoA-linked cinnamic acids Hypericum androsaemum 3 CoA + 2,4,6-trihydroxybenzophenone + 2 CO2
-
 ?
2.3.1.151 3 malonyl-CoA + 3-hydroxybenzoyl-CoA 3-hydroxybenzoyl-CoA is the preferred substrate Centaurium erythraea 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
-
 ?
2.3.1.177 2-hydroxybenzoyl-CoA + malonyl-CoA
-
 Sorbus aucuparia 4-hydroxycoumarin + CoA + CO2
-
 ?
2.3.1.177 malonyl-CoA + benzoyl-CoA
-
 Sorbus aucuparia CoA + 3,5-dihydroxybiphenyl + CO2
-
 ?
2.3.1.208 malonyl-CoA + 2-hydroxybenzoyl-CoA
-
 Sorbus aucuparia 2 CoA + 4-hydroxycoumarin + CO2
-
 ?
2.3.1.208 malonyl-CoA + 2-hydroxybenzoyl-CoA i.e. salicyl-CoA, reaction via an intermediate diketide Sorbus aucuparia 2 CoA + 4-hydroxycoumarin + CO2
-
 ?
2.3.1.208 additional information bifunctional enzyme, biphenyl synthase, BIS, catalyzes the formation of a linear tetraketide intermediate from benzoyl-CoA and three molecules of malonyl-CoA but uses an alternative intramolecular cyclization reaction to form 3,5-dihydroxybiphenyl, EC 2.3.1.177. When incubated with 2-hydroxybenzoyl (salicyl)-CoA, BIS catalyzes a single decarboxylative condensation with malonyl-CoA to form 4-hydroxycoumarin, EC 2.3.1.208 Sorbus aucuparia ?
-
 ?
2.3.1.208 additional information two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol Sorbus aucuparia ?
-
 ?
2.3.1.220 2 malonyl-CoA + benzoyl-CoA reaction of mutant T135L, no activity with the wild-type enzyme. The T135L mutant adds only two acetyl groups to the benzoyl starter unit to form a triketide intermediate which then cyclized into 6-phenyl-4-hydroxy-2-pyrone via C5 keto-enol oxygen -> C1 lactonization Sorbus aucuparia 3 CoA + 6-phenyl-4-hydroxy-2-pyrone + 2 CO2
-
 ?
2.3.1.220 3 malonyl-CoA + benzoyl-CoA
-
 Sorbus aucuparia 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
 ?
2.3.1.220 3 malonyl-CoA + benzoyl-CoA benzoyl-CoA is the preferred starter substrate of the wild-type enzyme, very low 2,4,6-trihydroxybenzophenone-forming activity with the mutant T135L Sorbus aucuparia 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
 ?
2.3.1.220 additional information 3-hydroxybenzoyl-CoA is the second best starter substrate for the wild-type enzyme but a poor starter molecule for the mutant enzyme T135L, resulting in formation of 2,3',4,6-tetrahydroxybenzophenone, reaction of EC 2.3.1.151. The benzoyl-primed triketides are covalently attached to the catalytic Cys167. The wild-type enzyme catalyzes another acetyl addition to the intermediate triketide Sorbus aucuparia ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.151 benzophenone synthase
-
 Centaurium erythraea
2.3.1.151 benzophenone synthase
-
 Hypericum androsaemum
2.3.1.151 BPS
-
 Centaurium erythraea
2.3.1.151 BPS
-
 Hypericum androsaemum
2.3.1.177 biphenyl synthase
-
 Sorbus aucuparia
2.3.1.177 BIS
-
 Sorbus aucuparia
2.3.1.208 biphenyl synthase
-
 Sorbus aucuparia
2.3.1.208 BIS
-
 Sorbus aucuparia
2.3.1.208 More cf. EC 2.3.1.177 Sorbus aucuparia
2.3.1.220 benzophenone synthase
-
 Sorbus aucuparia
2.3.1.220 BPS
-
 Sorbus aucuparia

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.151 35
-
-
 Hypericum androsaemum
2.3.1.220 35
-
-
 Sorbus aucuparia

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.151 0.055
-
 benzoyl-CoA
-
 Hypericum androsaemum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.151 6.5 7
-
 Hypericum androsaemum

Expression

EC Number Organism Comment Expression
2.3.1.177 Sorbus aucuparia BIS is only expressed when plant is infected with microorganisms up
2.3.1.208 Sorbus aucuparia elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicoyl-NAC) up

General Information

EC Number General Information Comment Organism
2.3.1.177 metabolism BIS is the key enzyme of biphenyl metabolism, producing for instance 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae. Sorbus aucuparia
2.3.1.208 evolution the enzyme belongs to the type III PKS superfamily of enzymes. In a phylogenetic tree, BIS and benzophenone synthase, BPS EC 2.3.1.151, group together closely, indicating that they arise from a relatively recent functional diversification of a common ancestral gene Sorbus aucuparia
2.3.1.208 physiological function when incubated with 2-hydroxybenzoyl (salicyl)-CoA, BIS catalyzes a single decarboxylative condensation with malonyl-CoA to form 4-hydroxycoumarin, also elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC). BIS is the key enzyme of biphenyl metabolism biphenyls and the related dibenzofurans are the phytoalexins of the Maloideae. Two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol, which is well-known for its blood anticoagulant activity and is the forerunner of medicinal anticoagulants Sorbus aucuparia
2.3.1.220 evolution 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 Sorbus aucuparia
2.3.1.220 malfunction 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 Sorbus aucuparia
2.3.1.220 metabolism BPS is the key enzyme of benzophenone metabolism Sorbus aucuparia
2.3.1.220 additional information the catalytic triad is formed by Cys167, His307, aand Asn340 Sorbus aucuparia

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.151 6.414
-
 benzoyl-CoA
-
 Hypericum androsaemum