Information on EC 2.3.1.177 - 3,5-dihydroxybiphenyl synthase

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The expected taxonomic range for this enzyme is: Maleae

EC NUMBER
COMMENTARY
2.3.1.177
-
RECOMMENDED NAME
GeneOntology No.
3,5-dihydroxybiphenyl synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
aldol condensation
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biphenyl synthase
-
-
biphenyl synthase
D2DRC4, D2DRC5, Q27Z07
enzyme belongs to the type III polyketide synthases
BIS
JQ390521
-
BIS
Q27Z07
enzyme belongs to the type III polyketide synthases
BIS1
Q27Z07
-
BIS2
H2FL89
-
BIS2
D2DRC4
enzyme belongs to the type III polyketide synthases, prefering 2-hydroxybenzoyl-CoA as a starter molecule instead of benzoyl-CoA
BIS3
H2FL90
-
BIS3
D2DRC5
enzyme belongs to the type III polyketide synthases, prefering 2-hydroxybenzoyl-CoA as a starter molecule instead of benzoyl-CoA
BIS4
H2FL91
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
BIS1; cvs. Holsteiner Cox and Cox Orange, genes MdBIS1
JQ390521
GenBank
Manually annotated by BRENDA team
BIS2; cvs. Holsteiner Cox and Cox Orange, gene MdBIS2
UniProt
Manually annotated by BRENDA team
BIS3; cvs. Holsteiner Cox and Cox Orange, gene MdBIS3
UniProt
Manually annotated by BRENDA team
BIS4; cvs. Holsteiner Cox and Cox Orange, gene MdBIS4
UniProt
Manually annotated by BRENDA team
enzyme expression is rapidly, strongly and transiently induced by yeast extract treatment
SwissProt
Manually annotated by BRENDA team
gene BIS1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the type-III polyketide synthase biphenyl synthase is encoded by a gene family, members of which are differentially regulated
evolution
H2FL89, H2FL90, H2FL91, JQ390521, -
biphenyl synthase, BIS, is a type III polyketide synthase; biphenyl synthase, BIS, is a type III polyketide synthase; biphenyl synthase, BIS, is a type III polyketide synthase; biphenyl synthase, BIS, is a type III polyketide synthase
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
D2DRC4, D2DRC5, Q27Z07
BIS is the key enzyme of biphenyl metabolism, producing for instance 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae.; BIS is the key enzyme of biphenyl metabolism, producing for instance 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae.; 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 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
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
H2FL89, H2FL90, H2FL91, JQ390521, -
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; 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; 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; 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
metabolism
-
biphenyl synthase 1 is the key enzyme of the biphenyl biosynthetic pathway and aucuparin accumulation
additional information
-
biphenyls exhibit stronger antibacterial activity than structurally related dibenzofurans do, occurrence of dibenzofuran phytoalexins in species of the Pyrinae, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxybenzoyl-CoA + malonyl-CoA
4-hydroxycoumarin + CoA + CO2
show the reaction diagram
-
-
-
-
?
2-hydroxybenzoyl-CoA + malonyl-CoA
4-hydroxycoumarin + CoA + CO2
show the reaction diagram
D2DRC4, D2DRC5, Q27Z07
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
show the reaction diagram
H2FL89, H2FL90, H2FL91, JQ390521, -
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 2-hydroxybenzoyl-CoA
CoA + 2-hydroxybenzoyltriacetic acid lactone + CO2
show the reaction diagram
-
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
show the reaction diagram
Q27Z07
52% of the activity with benzoyl-CoA
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
CoA + 3-hydroxycoumarin
show the reaction diagram
-
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
show the reaction diagram
Q27Z07
68% of the activity with benzoyl-CoA
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
D2DRC4, D2DRC5, Q27Z07
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
Q27Z07
-
low amounts of benzoyldiacetic acid lactone are synthesized as derailment product
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
-
enzyme is involved in the production of the phytoalexin aucuparin
-
-
?
malonyl-CoA + isobutyryl-CoA
CoA + ?
show the reaction diagram
-
5% of the activity with benzoyl-CoA without acidification, 15% of the activity with benzoyl-CoA with acidification
-
-
?
additional information
?
-
Q27Z07
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
?
-
H2FL89, H2FL90, H2FL91, 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
?
-
H2FL89, H2FL90, H2FL91, 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
?
-
H2FL89, H2FL90, H2FL91, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
show the reaction diagram
H2FL89, H2FL90, H2FL91, JQ390521, -
-
-
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
CoA + 3,5-dihydroxybiphenyl + CO2
show the reaction diagram
-
enzyme is involved in the production of the phytoalexin aucuparin
-
-
?
additional information
?
-
H2FL89, H2FL90, H2FL91, 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
?
-
H2FL89, H2FL90, H2FL91, 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
?
-
H2FL89, H2FL90, H2FL91, 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
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
benzoyl-CoA
H2FL89, H2FL90, H2FL91, JQ390521, -
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
H2FL89, H2FL90, H2FL91, 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DTT
-
stimulates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0008
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0023
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0032
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0007
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0014
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0016
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.7
-
benzoyl-CoA
Q27Z07
pH 7.0, 35°C
0.0062
-
malonyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.01
-
malonyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0101
-
malonyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
6.2
-
malonyl-CoA
Q27Z07
pH 7.0, 35°C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0045
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.02933
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.037
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.00717
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.0072
-
benzoyl-CoA
Q27Z07
pH 7.0, 35°C
0.01483
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
0.017
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.625
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
133985
11.49
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
133985
12.72
-
2-hydroxybenzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
133985
10.18
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
7389
10.63
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
7389
10.99
-
benzoyl-CoA
D2DRC4, D2DRC5, Q27Z07
-
7389
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
Q27Z07
-
6.5
7
D2DRC4, D2DRC5, Q27Z07
;
7
7.5
H2FL89, H2FL90, H2FL91, JQ390521, -
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
40
H2FL89, H2FL90, H2FL91, JQ390521, -
-
35
-
Q27Z07
-
35
-
D2DRC4, D2DRC5, Q27Z07
;
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.45
-
D2DRC4, D2DRC5, Q27Z07
-
6.42
-
D2DRC4, D2DRC5, Q27Z07
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
yeast-extract-treated
Manually annotated by BRENDA team
H2FL89, H2FL90, H2FL91, JQ390521, -
very low expression of BIS2
Manually annotated by BRENDA team
H2FL89, H2FL90, H2FL91, JQ390521, -
Erwinia amylovora infected; Erwinia amylovora infected; Erwinia amylovora infected, high expression levels of BIS3
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43000
-
D2DRC4, D2DRC5, Q27Z07
-
43100
-
D2DRC4, D2DRC5, Q27Z07
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
H2FL89, H2FL90, H2FL91, JQ390521, -
x * 43000, recombinant His-tagged BIS enzyme, SDS-PAGE; x * 43000, recombinant His-tagged BIS enzyme, SDS-PAGE; x * 43000, recombinant His-tagged BIS enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant N-terminally His6-tagged BIS2, BIS3, and BIS4 from Escherichia coli; recombinant N-terminally His6-tagged BIS3 from Escherichia coli; recombinant N-terminally His6-tagged BIS4 from Escherichia coli
H2FL89, H2FL90, H2FL91, JQ390521, -
purified by affinity chromatography on a nickel-nitrilotriacetic acid (Ni-NTA) agarose matrix; purified by affinity chromatography on a nickel-nitrilotriacetic acid (Ni-NTA) agarose matrix
D2DRC4, D2DRC5, Q27Z07
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene MdBIS1, DNA and amino acid sequence determination and analysis, phylogenetic tree, the BIS1 cDNA cloned from cv. Holsteiner Cox contains an early stop codon atposition 211 to 213 and does not yield a functional enzyme; gene MdBIS2, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of N-terminally His6-tagged BIS2 in Escherichia coli; gene MdBIS4, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of N-terminally His6-tagged BIS4 in Escherichia coli; genes MdBIS3, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of N-terminally His6-tagged BIS3 in Escherichia coli
H2FL89, H2FL90, H2FL91, JQ390521, -
expressed in Escherichia coli as N-terminally 6His-tagged protein; expressed in Escherichia coli as N-terminally 6His-tagged protein
D2DRC4, D2DRC5, Q27Z07
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
infection with Erwinia amylovora induces the enzyme; infection with Erwinia amylovora induces the enzyme. In cell cultures of apple cultivar Cox Orange, expression of BIS2 gene is observed after the addition of an autoclaved Erwinia amylovora suspension, BIS3 protein is accumulated in the transition zone of stems in the parenchyma of the bark at the junctions between neighboring cortical parenchyma cells; the BIS3 gene is reduced in response to inoculation with Erwinia amylovora in stems of cv. Holsteiner Cox with highest transcript levels in the transition zone between necrotic and healthy tissues. In cell cultures of apple cultivar Cox Orange, expression of BIS3 gene is observed after the addition of an autoclaved Erwinia amylovora suspension, BIS3 protein is accumulated in the transition zone of stems in the parenchyma of the bark at the junctions between neighboring cortical parenchyma cells
H2FL89, H2FL90, H2FL91, JQ390521, -
the enzyme is induced by elicitors
-
BIS is only expressed when plant is infected with microorganisms
-
the enzyme is induced by elicitors
-
addition of yeast extract to the cell cultures results in a burst of reactive oxygen species, H2O2 and O2-, followed by transcriptional activation of the biphenyl synthase 1 gene BIS1. Endogenous generation of H2O2, by superoxide dismutase, rather than that of O2- is akey factor in YE-induced accumulation of biphenyl phytoalexins in cell cultures of Sorbus aucuparia
-