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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonyl-CoA + 2-hydroxybenzoyl-CoA | Sorbus aucuparia | - |
2 CoA + 4-hydroxycoumarin + CO2 | - |
? | |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sorbus aucuparia | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | elicitor-treated | Sorbus aucuparia | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonyl-CoA + 2-hydroxybenzoyl-CoA | - |
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 | ? | - |
? | |
additional information | two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol | Sorbus aucuparia | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
biphenyl synthase | - |
Sorbus aucuparia |
BIS | - |
Sorbus aucuparia |
More | cf. EC 2.3.1.177 | Sorbus aucuparia |
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 | 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 |