2.3.1.208	malonyl-CoA + 2-hydroxybenzoyl-CoA	-	Malus domestica	2 CoA + 4-hydroxycoumarin + CO2	-	?	419454	
2.3.1.208	malonyl-CoA + 2-hydroxybenzoyl-CoA	-	Sorbus aucuparia	2 CoA + 4-hydroxycoumarin + CO2	-	?	419454	
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	-	?	419454	
2.3.1.208	malonyl-CoA + 3-hydroxybenzoyl-CoA	-	Sorbus aucuparia	2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2	-	?	419455	
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	?	-	?	89	
2.3.1.208	additional information	biphenyl synthase isozyme BIS1, in contrast to isozymes BIS2 and BIS3, does not prefer 2-hydroxybenzoyl (salicyl)-CoA as a starter substrat, but also catalyzes a single decarboxylative condensation with malonyl-CoA to give 4-hydroxycoumarin	Sorbus aucuparia	?	-	?	89	
2.3.1.208	additional information	for the bifunctional BIS, the preferred starter substrates are benzoyl-CoA and salicoyl-CoA, leading to the formation of 3,5-dihydroxybiphenyl and 4-hydroxycoumarin, EC 2.3.1.177 and 2.3.1.208, respectively, in the presence of malonyl-CoA as extender molecule	Malus domestica	?	-	?	89	
2.3.1.208	additional information	for the bifunctional BIS, the preferred starter substrates are benzoyl-CoA and salicoyl-CoA, leading to the formation of 3,5-dihydroxybiphenyl and 4-hydroxycoumarin, EC 2.3.1.177 and 2.3.1.208, respectively, in the presence of malonyl-CoA as extender molecule	Sorbus aucuparia	?	-	?	89	
2.3.1.208	additional information	in contrast to isozyme BIS1, biphenyl synthase isoenzymes BIS2 and BIS3 prefer ortho-hydroxybenzoyl (salicyl)-CoA as a starter substrate and catalyze a single decarboxylative condensation with malonyl-CoA to give 4-hydroxycoumarin	Sorbus aucuparia	?	-	?	89	
2.3.1.208	additional information	substrate specificities of BIS isoenzymes from cell cultures, overview. The bifunctional enzyme also forms 3,5-dihydroxybiphenyl from malonyl-CoA and benzoyl-CoA, reaction of biphenyl synthase, EC 2.3.1.177. When benzoyl-CoA is replaced with salicyl-CoA as a starter substrate, the enzyme catalyzes a single decarboxylative condensation reaction with malonyl-CoA to form a diketide intermediate which undergoes intramolecular cyclization by nucleophilic attack of the phenol group on the CoA- or cysteine-tethered C-1 thioester, yielding 4-hydroxycoumarin after enolization. No activity with 4-hydroxybenzoyl-CoA, cinnamoyl-CoA, 2-coumaroyl-CoA, 3-coumaroyl-CoA, 4-coumaroyl-CoA, and acetyl-CoA or with free salicylic acid or 2-coumaric acid	Sorbus aucuparia	?	-	?	89