2.3.1.177: 3,5-dihydroxybiphenyl synthase
This is an abbreviated version!
For detailed information about 3,5-dihydroxybiphenyl synthase, go to the full flat file.
Word Map on EC 2.3.1.177
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2.3.1.177
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biphenyls
-
phytoalexins
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dibenzofurans
-
sorbus
-
apple
-
aucuparin
-
polyketide
-
pear
-
elicitor-treated
-
starter
-
elicitors
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rosaceae
-
malus
-
maloideae
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subtribe
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benzoic
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domestica
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blight
-
pyrus
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amylovora
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benzophenone
-
pyrinae
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inaequalis
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4-hydroxylation
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venturia
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4-hydroxycoumarin
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rootstock
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dot-shaped
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delicious
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replant
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rosaceous
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dicoumarol
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greenhouse-grown
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n-acetylcysteamine
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4-coumaroyl-coa
-
pyrifolia
-
scab-causing
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benzoate-coa
-
rowan
-
scab
- 2.3.1.177
- biphenyls
-
phytoalexins
- dibenzofurans
-
sorbus
- apple
-
aucuparin
- polyketide
- pear
-
elicitor-treated
-
starter
- elicitors
- rosaceae
- malus
- maloideae
-
subtribe
-
benzoic
- domestica
-
blight
- pyrus
- amylovora
- benzophenone
-
pyrinae
- inaequalis
-
4-hydroxylation
-
venturia
- 4-hydroxycoumarin
-
rootstock
-
dot-shaped
-
delicious
-
replant
-
rosaceous
- dicoumarol
-
greenhouse-grown
- n-acetylcysteamine
- 4-coumaroyl-coa
- pyrifolia
-
scab-causing
-
benzoate-coa
- rowan
-
scab
Reaction
3 malonyl-CoA
+
Synonyms
biphenyl synthase, BIS, BIS1, BIS1 biphenyl synthase, BIS2, BIS3, BIS3 biphenyl synthase, BIS4, MdBIS1, MdBIS3, PcBIS1, PcBIS2
ECTree
2.3.1.177 3,5-dihydroxybiphenyl synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.1.177 - 3,5-dihydroxybiphenyl synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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 + isobutyryl-CoA
CoA + ?
-
5% of the activity with benzoyl-CoA without acidification, 15% of the activity with benzoyl-CoA with acidification
-
-
?
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
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
-
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
-
-
-
-
?
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
-
-
?
