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2-hydroxybenzoyl-CoA + malonyl-CoA
4-hydroxycoumarin + CoA + CO2
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
3 malonyl-CoA + salicoyl-CoA
4 CoA + 4-hydroxycoumarin + 4 CO2
benzoyldiacetic acid lactone (6-phenyl-4-hydroxy-2-pyrone) is formed as a minor by-product
-
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
CoA + 2-hydroxybenzoyltriacetic acid lactone + CO2
malonyl-CoA + 3-hydroxybenzoyl-CoA
CoA + 3-hydroxycoumarin
-
8% of the activity with benzoyl-CoA without acidification, 22% of the activity with benzoyl-CoA with acidification
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
CoA + ? + CO2
68% of the activity with benzoyl-CoA
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
malonyl-CoA + isobutyryl-CoA
CoA + ?
-
5% of the activity with benzoyl-CoA without acidification, 15% of the activity with benzoyl-CoA with acidification
-
-
?
additional information
?
-
2-hydroxybenzoyl-CoA + malonyl-CoA
4-hydroxycoumarin + CoA + CO2
-
-
-
-
?
2-hydroxybenzoyl-CoA + malonyl-CoA
4-hydroxycoumarin + CoA + CO2
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
benzoyldiacetic acid lactone (6-phenyl-4-hydroxy-2-pyrone) is formed as a minor by-product
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
the enzyme is involved in biphenyl biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
CoA + 2-hydroxybenzoyltriacetic acid lactone + CO2
-
11% of the activity with benzoyl-CoA without acidification, 86% of the activity with benzoyl-CoA with acidification
derailment product
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
CoA + 2-hydroxybenzoyltriacetic acid lactone + CO2
52% of the activity with benzoyl-CoA
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
low amounts of benzoyldiacetic acid lactone are synthesized as derailment product
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
enzyme is involved in the production of the phytoalexin aucuparin
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
benzoyl-CoA is the preferred starter substrate. Enzyme does not accept 4-hydroxybenzoyl-CoA or CoA-linked cinnamic acids such as 4-coumaroyl-CoA
-
-
?
additional information
?
-
-
benzoyl-CoA is the preferred starter substrate. Enzyme does not accept 4-hydroxybenzoyl-CoA or CoA-linked cinnamic acids such as 4-coumaroyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
additional information
?
-
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
the enzyme is involved in biphenyl biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
-
enzyme is involved in the production of the phytoalexin aucuparin
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS2 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS3 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
JQ390521
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 2.3.1.208, 4-hydroxycoumarin synthase, with malonyl-CoA and 2-hydroxybenzoyl-CoA, i.e. salicoyl-CoA, as substrates forming 4-hydroxycoumarin, no formation of 2',3,5-trihydroxybiphenyl. BIS4 exhibits highest affinity for benzoyl-CoA. The turnover rate is slightly higher with salicoyl-CoA
-
-
?
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evolution
biphenyl synthase, BIS, is a type III polyketide synthase
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica. The results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants
metabolism
-
BIS is the key enzyme of biphenyl metabolism, producing for instance 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae.
metabolism
BIS is the key enzyme of biphenyl metabolism, producing for instance 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae.
metabolism
-
biphenyl synthase 1 is the key enzyme of the biphenyl biosynthetic pathway and aucuparin accumulation
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin
metabolism
-
biphenyl synthase is the key enzyme that forms the carbon skeleton, it is involved in biosynthesis of aucuparin. Biosynthetic reactions leading to biphenyl and dibenzofuran phytoalexins in cell cultures of Sorbus aucuparia, overview
metabolism
-
the enzyme is involved in biphenyl biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
physiological function
biphenyl synthase is induced by elicitors, e.g. phytopathogen infection. In stems infected with Erwinia amylovora the transition zone between necrotic and healthy tissues is the accumulation site of biphenyl and dibenzofuran phytoalexins and of expression of biphenyl synthase
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
physiological function
-
biphenyls, whose biosynthesis involves the biphenyl synthase, and dibenzofurans are the phytoalexins of the Pyrinae, corresponding to the Maloideae, a subfamily of the plant family Rosaceae. Occurrence of biphenyl phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
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Liu, B.; Beuerle, T.; Klundt, T.; Beerhues, L.
Biphenyl synthase from yeast-extract-treated cell cultures of Sorbus aucuparia
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Sorbus aucuparia
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Liu, B.; Raeth, T.; Beuerle, T.; Beerhues, L.
Biphenyl synthase, a novel type III polyketide synthase
Planta
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2007
Sorbus aucuparia (Q27Z07), Sorbus aucuparia
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Beerhues, L.; Liu, B.; Raeth, T.; Klundt, T.; Beuerle, T.; Bocola, M.
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Sorbus aucuparia
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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
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Liu, B.; Raeth, T.; Beuerle, T.; Beerhues, L.
A novel 4-hydroxycoumarin biosynthetic pathway
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Sorbus aucuparia (D2DRC4), Sorbus aucuparia (D2DRC5), Sorbus aucuparia (Q27Z07), Sorbus aucuparia
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Chizzali, C.; Beerhues, L.
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Chaenomeles japonica, Rhaphiolepis bibas, Malus domestica, Malus sylvestris, Pyrus communis, Sorbus aucuparia, Photinia glabra, Rhaphiolepis umbellata, Aronia arbutifolia, Chaenomeles cathayensis, Malus sieversii
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Chizzali, C.; Gaid, M.M.; Belkheir, A.K.; Haensch, R.; Richter, K.; Flachowsky, H.; Peil, A.; Hanke, M.V.; Liu, B.; Beerhues, L.
Differential expression of biphenyl synthase gene family members in fire-blight-infected apple Holsteiner Cox
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2012
Malus domestica (H2FL89), Malus domestica (H2FL90), Malus domestica (H2FL91), Malus domestica (JQ390521), Malus domestica
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Qiu, X.; Lei, C.; Huang, L.; Li, X.; Hao, H.; Du, Z.; Wang, H.; Ye, H.; Beerhues, L.; Liu, B.
Endogenous hydrogen peroxide is a key factor in the yeast extract-induced activation of biphenyl biosynthesis in cell cultures of Sorbus aucuparia
Planta
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2012
Sorbus aucuparia
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Reckwell, D.; Haensch, R.; Schulze, J.; Beerhues, L.
Immunolocalization of biphenyl synthase in elicitor-treated cell cultures of Sorbus aucuparia
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2014
Sorbus aucuparia (Q27Z07)
-
brenda
Khalil, M.N.; Brandt, W.; Beuerle, T.; Reckwell, D.; Groeneveld, J.; Haensch, R.; Gaid, M.M.; Liu, B.; Beerhues, L.
O-Methyltransferases involved in biphenyl and dibenzofuran biosynthesis
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2015
Sorbus aucuparia (Q27Z07), Sorbus aucuparia
brenda
Stewart, C.; Woods, K.; Macias, G.; Allan, A.C.; Hellens, R.P.; Noel, J.P.
Molecular architectures of benzoic acid-specific type III polyketide synthases
Acta Crystallogr. Sect. D
73
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2017
Malus domestica (K9MS05), Malus domestica (K9MST3)
brenda
Saini, S.S.; Teotia, D.; Gaid, M.; Thakur, A.; Beerhues, L.; Sircar, D.
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2017
Pyrus pyrifolia
brenda
Chizzali, C.; Swiddan, A.K.; Abdelaziz, S.; Gaid, M.; Richter, K.; Fischer, T.C.; Liu, B.; Beerhues, L.
Expression of biphenyl synthase genes and formation of phytoalexin compounds in three fire blight-infected Pyrus communis cultivars
PLoS ONE
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2016
Pyrus communis (A0A1B1PJB0), Pyrus communis (A0A1B1PJB7), Pyrus communis
brenda