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Information on EC 2.3.1.177 - 3,5-dihydroxybiphenyl synthase
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EC Tree
2.3.1.177 3,5-dihydroxybiphenyl synthaseIUBMB Comments
A polyketide synthase that is involved in the production of the phytoalexin aucuparin. 2-Hydroxybenzoyl-CoA can also act as substrate but it leads to the derailment product 4-hydroxycoumarin (cf. EC 2.3.1.208, 4-hydroxycoumarin synthase) . This enzyme uses the same starter substrate as EC 2.3.1.151, benzophenone synthase.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
biphenyl synthase, pcbis2, pcbis1, mdbis1, mdbis3, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
biphenyl synthase
BIS
BIS1
BIS2
BIS3
biphenyl synthase
enzyme belongs to the type III polyketide synthases
BIS2
enzyme belongs to the type III polyketide synthases, prefering 2-hydroxybenzoyl-CoA as a starter molecule instead of benzoyl-CoA
BIS3
enzyme belongs to the type III polyketide synthases, prefering 2-hydroxybenzoyl-CoA as a starter molecule instead of benzoyl-CoA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:benzoyl-CoA malonyltransferase
A polyketide synthase that is involved in the production of the phytoalexin aucuparin. 2-Hydroxybenzoyl-CoA can also act as substrate but it leads to the derailment product 4-hydroxycoumarin (cf. EC 2.3.1.208, 4-hydroxycoumarin synthase) [2]. This enzyme uses the same starter substrate as EC 2.3.1.151, benzophenone 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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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 + 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
-
-
-
-
?
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzoyl-CoA
benzoyl-CoA causes inhibition of BIS2 activity at concentrations above 0.015 mM; benzoyl-CoA causes inhibition of BIS3 activity at concentrations above 0.015 mM; benzoyl-CoA causes inhibition of BIS4 activity at concentrations above 0.015 mM
additional information
no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM
-
additional information
no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM
-
additional information
no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM
-
additional information
JQ390521
no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM
-
additional information
-
no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM; no substrate inhibition by salicoyl-CoA up to 0.05 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Expression of Biphenyl Synthase Genes and Formation of Phytoalexin Compounds in Three Fire Blight-Infected Pyrus communis Cultivars.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
7 - 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
BIS1; cvs. Holsteiner Cox and Cox Orange, genes MdBIS1
JQ390521
GenBank
brenda