2.3.1.208	malonyl-CoA + 2-hydroxybenzoyl-CoA	-	
2.3.1.208	malonyl-CoA + 3-hydroxybenzoyl-CoA	-	
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	
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	
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	
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