BRENDA - Enzyme Database
show all sequences of 2.3.1.208

A novel 4-hydroxycoumarin biosynthetic pathway

Liu, B.; Raeth, T.; Beuerle, T.; Beerhues, L.; Plant Mol. Biol. 72, 17-25 (2010)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
isozyme BIS2, cDNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged isozyme; isozyme BIS3, cDNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged isozyme
Sorbus aucuparia
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0008
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.0023
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.0032
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
0.0062
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.01
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.0101
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43100
-
x * 43100, about, BIS2, sequence calculation
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
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
Sorbus aucuparia
-
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
-
-
?
additional information
Sorbus aucuparia
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
?
-
-
-
additional information
Sorbus aucuparia
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
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Sorbus aucuparia
D2DRC4
BIS2; isozyme BIS2
-
Sorbus aucuparia
D2DRC5
BIS3; isozyme BIS3
-
Sorbus aucuparia
-
isozyme BIS1
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged BIS2 by nickel affinity chromatography; recombinant His-tagged BIS3 by nickel affinity chromatography
Sorbus aucuparia
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
elicitor-treated; elicitor-treated; 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
-
706258
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
-
706258
Sorbus aucuparia
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
-
-
-
?
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 4300, about, BIS3, sequence calculation; x * 43100, about, BIS2, sequence calculation
Sorbus aucuparia
Synonyms
Synonyms
Commentary
Organism
BIS1
-
Sorbus aucuparia
BIS2
-
Sorbus aucuparia
BIS3
-
Sorbus aucuparia
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
-
-
Sorbus aucuparia
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0045
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.029
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.037
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Sorbus aucuparia
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Sorbus aucuparia
BIS2, sequence calculation
-
5.45
Sorbus aucuparia
BIS3, sequence calculation
-
6.42
Cloned(Commentary) (protein specific)
Commentary
Organism
isozyme BIS2, cDNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged isozyme
Sorbus aucuparia
isozyme BIS3, cDNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged isozyme
Sorbus aucuparia
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0008
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.0023
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.0032
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
0.0062
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.01
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.0101
-
malonyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43100
-
x * 43100, about, BIS2, sequence calculation
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
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
Sorbus aucuparia
-
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
-
-
?
additional information
Sorbus aucuparia
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
?
-
-
-
additional information
Sorbus aucuparia
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
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged BIS2 by nickel affinity chromatography
Sorbus aucuparia
recombinant His-tagged BIS3 by nickel affinity chromatography
Sorbus aucuparia
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
-
706258
Sorbus aucuparia
2 CoA + 4-hydroxycoumarin + CO2
-
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
-
706258
Sorbus aucuparia
2 CoA + 2-oxabicyclo[4.3.1]deca-1(10),6,8-triene-3,5-dione + CO2
-
-
-
?
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
additional information
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
706258
Sorbus aucuparia
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 43100, about, BIS2, sequence calculation
Sorbus aucuparia
?
x * 4300, about, BIS3, sequence calculation
Sorbus aucuparia
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
-
-
Sorbus aucuparia
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0045
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
0.029
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
0.037
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Sorbus aucuparia
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Sorbus aucuparia
BIS2, sequence calculation
-
5.45
Sorbus aucuparia
BIS3, sequence calculation
-
6.42
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 (salicyl-NAC), elicitors induce BIS2, expression profile, overview; elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC), elicitors induce BIS3, expression profile, overview
up
General Information
General Information
Commentary
Organism
additional information
the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs; the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs; the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs
Sorbus aucuparia
physiological function
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC); elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC); elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC)
Sorbus aucuparia
General Information (protein specific)
General Information
Commentary
Organism
additional information
the isozyme contains the Cys-His-Asn catalytic triad conserved in type III PKSs
Sorbus aucuparia
physiological function
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC)
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 (salicyl-NAC), elicitors induce BIS2, expression profile, overview
up
Sorbus aucuparia
elicitor-treated cell cultures of Sorbus aucuparia form 4-hydroxycoumarin when fed with the N-acetylcysteamine thioester of salicylic acid (salicyl-NAC), elicitors induce BIS3, expression profile, overview
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.625
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
11.49
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
12.72
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.625
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS1
Sorbus aucuparia
11.49
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS3
Sorbus aucuparia
12.72
-
2-hydroxybenzoyl-CoA
pH 6.5-7.0, 35C, BIS2
Sorbus aucuparia
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
-
-