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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
malonyl-CoA + 3-hydroxybenzoyl-CoA
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
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additional information
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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i.e. salicyl-CoA, reaction via an intermediate diketide
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additional information
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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
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additional information
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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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additional information
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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
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additional information
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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
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additional information
?
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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
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additional information
?
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
malonyl-CoA + 3-hydroxybenzoyl-CoA
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
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additional information
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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malonyl-CoA + 2-hydroxybenzoyl-CoA
2 CoA + 4-hydroxycoumarin + CO2
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additional information
?
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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
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additional information
?
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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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additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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evolution
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biphenyl synthase is a type III polyketide synthase
evolution
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biphenyl synthase is a type III polyketide synthase
evolution
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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
physiological function
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BIS3 appears to catalyze the formation of phytoalexins in the transition zone, while BIS2 does not
physiological function
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC)
physiological function
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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
additional information
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the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs
additional information
the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs
additional information
the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs
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Beerhues, L.; Liu, B.
Biosynthesis of biphenyls and benzophenones-evolution of benzoic acid-specific type III polyketide synthases in plants
Phytochemistry
70
1719-1727
2009
Sorbus aucuparia
brenda
Liu, B.; Raeth, T.; Beuerle, T.; Beerhues, L.
A novel 4-hydroxycoumarin biosynthetic pathway
Plant Mol. Biol.
72
17-25
2010
Sorbus aucuparia, Sorbus aucuparia (D2DRC4), Sorbus aucuparia (D2DRC5)
brenda
Chizzali, C.; Gaid, M.M.; Belkheir, A.K.; Beuerle, T.; Haensch, R.; Richter, K.; Flachowsky, H.; Peil, A; Hanke, M.-V.; Liu, B.; Beerhues, L.
Phytoalexin formation in fire blight-infected apple
Trees
2012
1-8
2012
Malus domestica, Sorbus aucuparia
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brenda