BRENDA - Enzyme Database
show all sequences of 2.3.1.208

Biosynthesis of biphenyls and benzophenones-evolution of benzoic acid-specific type III polyketide synthases in plants

Beerhues, L.; Liu, B.; Phytochemistry 70, 1719-1727 (2009)

Data extracted from this reference:

Engineering
Protein Variants
Commentary
Organism
S338G
CHS numbering, site-directed mutagenesis of the mechanistically important residue
Sorbus aucuparia
T132A
CHS numbering, site-directed mutagenesis of the mechanistically important residue
Sorbus aucuparia
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
malonyl-CoA + 2-hydroxybenzoyl-CoA
Sorbus aucuparia
-
2 CoA + 4-hydroxycoumarin + CO2
-
-
?
additional information
Sorbus aucuparia
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
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Sorbus aucuparia
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
elicitor-treated
Sorbus aucuparia
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
malonyl-CoA + 2-hydroxybenzoyl-CoA
-
706131
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
i.e. salicyl-CoA, reaction via an intermediate diketide
706131
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
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
706131
Sorbus aucuparia
?
-
-
-
-
additional information
two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol
706131
Sorbus aucuparia
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
biphenyl synthase
-
Sorbus aucuparia
BIS
-
Sorbus aucuparia
More
cf. EC 2.3.1.177
Sorbus aucuparia
Engineering (protein specific)
Protein Variants
Commentary
Organism
S338G
CHS numbering, site-directed mutagenesis of the mechanistically important residue
Sorbus aucuparia
T132A
CHS numbering, site-directed mutagenesis of the mechanistically important residue
Sorbus aucuparia
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
malonyl-CoA + 2-hydroxybenzoyl-CoA
Sorbus aucuparia
-
2 CoA + 4-hydroxycoumarin + CO2
-
-
?
additional information
Sorbus aucuparia
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
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
elicitor-treated
Sorbus aucuparia
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
malonyl-CoA + 2-hydroxybenzoyl-CoA
-
706131
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
i.e. salicyl-CoA, reaction via an intermediate diketide
706131
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
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
706131
Sorbus aucuparia
?
-
-
-
-
additional information
two molecules of 4-hydroxycoumarin spontaneously combine with formaldehyde to give dicoumarol
706131
Sorbus aucuparia
?
-
-
-
-
Expression
Organism
Commentary
Expression
Sorbus aucuparia
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicoyl-NAC)
up
General Information
General Information
Commentary
Organism
evolution
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
Sorbus aucuparia
physiological function
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
Sorbus aucuparia
General Information (protein specific)
General Information
Commentary
Organism
evolution
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
Sorbus aucuparia
physiological function
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
Sorbus aucuparia
Expression (protein specific)
Organism
Commentary
Expression
Sorbus aucuparia
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicoyl-NAC)
up
Other publictions for EC 2.3.1.208
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721091
Chizzali
-
Phytoalexin formation in fire ...
Malus domestica, Sorbus aucuparia
Trees
2012
1-8
2012
-
-
-
-
-
-
-
-
1
-
1
4
-
2
-
-
-
-
-
5
-
-
4
1
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
4
-
-
-
-
-
5
-
-
4
1
-
-
-
-
-
-
-
-
2
3
3
2
-
-
706258
Liu
A novel 4-hydroxycoumarin bios ...
Sorbus aucuparia
Plant Mol. Biol.
72
17-25
2010
-
-
1
-
-
-
-
6
-
-
1
8
-
3
-
-
1
-
-
1
-
-
11
1
3
1
-
-
3
1
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
-
6
-
-
1
8
-
-
-
2
-
3
-
-
11
2
3
-
-
3
3
-
-
2
1
2
6
2
3
3
706131
Beerhues
Biosynthesis of biphenyls and ...
Sorbus aucuparia
Phytochemistry
70
1719-1727
2009
-
-
-
-
2
-
-
-
-
-
-
2
-
1
-
-
-
-
-
1
-
-
4
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
1
2
2
1
-
-