Information on EC 2.3.1.159 - acridone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.159
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RECOMMENDED NAME
GeneOntology No.
acridone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acridone alkaloid biosynthesis
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Acridone alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing)
Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis)
CAS REGISTRY NUMBER
COMMENTARY hide
99085-53-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone+ 3 CO2
show the reaction diagram
-
enzyme accepts 4-coumaroyl-CoA as a starter substrate to yield naringenin chalcone, along with triketide and tetraketide lactone derailment by-products
-
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + benzophenone + 3 CO2
show the reaction diagram
-
-
-
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + phloroglucinol + 3 CO2
show the reaction diagram
-
-
-
?
3 malonyl-CoA + N-methylanthraniloyl-CoA
4 CoA + 1,3-dihydroxy-N-methylacridone + N-methylanthraniloyltriacetic acid lactone + 4-hydroxy-N-methylquinolone + 3 CO2
show the reaction diagram
-
enzyme accepts N-methylanthraniloyl-CoA as the starter substrate to produce the tetraketide 1,3-dihydroxy-N-methylacridone after sequential condensations with three molecules of malonyl-CoA, along with 4-hydroxy-N-methylquinolone and N-methylanthraniloyltriacetic acid lactone. The catalytic efficiency for the formation of the acridone is 2.8fold higher than that of the quinolone
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
small amounts of bisnoryangonin and 4-coumaroyltriacetic acid lactone are formed as byproducts
-
?
4-methoxycinnamoyl-CoA + 3 malonyl-CoA
4-methoxy-2',4',6'-trihydroxychalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-methoxycinnamoyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
-
-
-
?
acetyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
-
-
-
?
benzoyl-CoA + malonyl-CoA
2,3',4,6-tetrahydroxybenzophenone + CoA + CO2
show the reaction diagram
-
-
-
?
hexanoyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
CoA + naringenin chalcone
show the reaction diagram
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
show the reaction diagram
N-methylanthraniloyl-CoA + Malonyl-CoA
1,3-dihydroxy-N-methylacridone + CoA + CO2
show the reaction diagram
N-methylanthraniloyl-CoA + malonyl-CoA
N-methylacridone + CoA + CO2
show the reaction diagram
-
-
-
?
phenylacetyl-CoA + malonyl-CoA
2,4,6-trihydroxyphenylbenzylketone + CoA + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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0.5 mM: 95% inhibition
N-ethylmaleimide
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1 mM: 100% inhibition
p-chloromercuribenzoate
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0.5 mM: 95% inhibition
additional information
-
light irradiation decreases activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
induced activity by addition of crude elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea, syn. Phytophthora sojae
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0136 - 19.7
4-Coumaroyl-CoA
0.005 - 0.0328
malonyl-CoA
0.0043 - 0.077
N-methylanthraniloyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 0.113
4-Coumaroyl-CoA
0.023 - 0.067
N-methylanthraniloyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.33
4-Coumaroyl-CoA
Citrus x microcarpa
U3KRF0
pH 7.0, 30°C
448
1.95 - 5.4
N-methylanthraniloyl-CoA
5819
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.18
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crude extract
6.035
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purified enzyme
9.54
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purified recombinant isozyme I
14.16
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purified recombinant isozyme II
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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isozyme II
7.5
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isozyme I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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isozyme II, assay range
6 - 9
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isozyme I, assay range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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isozyme II
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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endodermis and vascular tissue, mRNA and protein
Manually annotated by BRENDA team
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adjacent to the rhizodermis, mRNA and protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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about, isozyme II, gel filtration
69000
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gel filtration
81000
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isozyme I, analytical ultracentrifugation
82000
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isozyme II, analytical ultracentrifugation
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45831, calculated
monomer
1 * 42000, recombinant enzyme from Escherichia coli, SDS-PAGE and western blot analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.35 A resolution. Structure reveals wide active site entrances providing sufficient space to facilitate the binding of the bulky N-methylanthraniloyl-CoA within the catalytic center
using the hanging-drop vapour-diffusion method
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, partially purified, stable for at least 4 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the recombinant protein by glutathione sepharose affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli with an additional hexahistidine tag at the N-terminus
expression in Escherichia coli
expression in Escherichia coli strain BL21 (DE3)pLys S and in lambda phages via Escherichia coli host, DNA sequence comparison of 4 clones and also with the DNA sequence of Ruta graveolens chalcone synthase
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expression in Escherichia coli strain BL21 (DE3)pLys S and in lambda phages via Escherichia coli host, DNA sequence determination; expression level in Escherichia coli is decreased by light irradiation and increased by treatment with elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea
expression in Escherichia coli strain M15
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expression of wild-type and mutants in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S132T/A133S/V265F
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site-directed mutagenesis, exchange of 3 residues, responsible for substrate activity, by the corresponding amino acids of chalcone synthase results in transformation of the enzyme to a chalcone synthase, 25fold increased activity, with only 36% remaining acridone synthase activity compared to wild-type
V265F
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site-directed mutagenesis, 75% reduction of ACS catalytic activity, but 2fold increased chalcone synthase activity
additional information
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the starter substrates for chalcone synthase or acridone synthase reaction are placed in different topographies in the active site pocket of the enzymes. Therefore conformational changes in the periphery beyond the active site cavity volumes determine the product formation and interconversion of enzymes by mutation of the active sites is insufficient