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Literature summary for 2.3.1.208 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
Search for more literature for 2.3.1.208

Protein Variants

Protein Variants Comment Organism
S338G CHS numbering, site-directed mutagenesis of the mechanistically important residue Sorbus aucuparia
T132A CHS numbering, site-directed mutagenesis of the mechanistically important residue Sorbus aucuparia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
malonyl-CoA + 2-hydroxybenzoyl-CoA Sorbus aucuparia
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 2 CoA + 4-hydroxycoumarin + CO2
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 ?
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 ?
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 ?

Organism

Organism UniProt Comment Textmining
Sorbus aucuparia
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture elicitor-treated Sorbus aucuparia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonyl-CoA + 2-hydroxybenzoyl-CoA
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 Sorbus aucuparia 2 CoA + 4-hydroxycoumarin + CO2
-
 ?
malonyl-CoA + 2-hydroxybenzoyl-CoA i.e. salicyl-CoA, reaction via an intermediate diketide Sorbus aucuparia 2 CoA + 4-hydroxycoumarin + CO2
-
 ?
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 ?
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 ?
additional information two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol Sorbus aucuparia ?
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 ?

Synonyms

Synonyms Comment Organism
biphenyl synthase
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 Sorbus aucuparia
BIS
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 Sorbus aucuparia
More cf. EC 2.3.1.177 Sorbus aucuparia

Expression

Organism Comment Expression
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

General Information Comment Organism
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
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