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Information on EC 2.3.1.159 - acridone synthase
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2.3.1.159 acridone synthaseIUBMB Comments
Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis)
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Word Map
- 2.3.1.159
- chalcone
- polyketide
- graveolens
- malonyl-coas
- synthases
-
starter
- benzophenone
- rutaceae
- 4-coumaroyl-coa
-
citrus
-
condensations
- phloroglucinols
- stilbene
-
tetraketides
-
bibenzyl
- anthranilate
-
quinolone
-
plant-specific
-
2-pyrone
- serrata
- huperzia
-
moss
-
club
- naringenin
- microcarpa
The enzyme appears in viruses and cellular organisms
Synonyms
acridone synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acridone synthase
ACS
PKS1
-
type III polyketide synthase has 58% identity with acridone synthase from Ruta graveolens
synthatase, acridone (9Cl)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 + H2O
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 + H2O
two-step mechanism
-
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 + H2O
Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases
-
-
-
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 + H2O
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
condensation
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PATHWAY SOURCE
PATHWAYS
-
-
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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)
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CAS REGISTRY NUMBER
COMMENTARY
99085-53-7
-
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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 + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
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 + hexanoyl-CoA
4 CoA + phloroglucinol + 3 CO2
-
-
-
?
3 malonyl-CoA + N-methylanthraniloyl-CoA
4 CoA + 1,3-dihydroxy-N-methylacridone + N-methylanthraniloyltriacetic acid lactone + 4-hydroxy-N-methylquinolone + 3 CO2
-
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 + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
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
-
-
-
-
?
benzoyl-CoA + malonyl-CoA
2,3',4,6-tetrahydroxybenzophenone + CoA + CO2
-
-
-
?
N-methylanthraniloyl-CoA + 3 malonyl-CoA
1,3-dihydroxy-N-methylacridone + 4 CoA + 3 CO2
-
-
-
?
phenylacetyl-CoA + malonyl-CoA
2,4,6-trihydroxyphenylbenzylketone + CoA + CO2
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
CoA + naringenin chalcone
-
isozyme I shows 16% activity and isozyme II shows 12% activity compared to the activity with N-methylanthraniloyl-CoA as substrate, respectively
-
?
malonyl-CoA + 4-coumaroyl-CoA
CoA + naringenin chalcone
-
wild-type shows low activity, while mutants show highly increased activity
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
activity is increased upon treatment with crude elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea, syn. Phytophthora sojae, and decreased upon light irradiation
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
activity is increased upon treatment with crude elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea, syn. Phytophthora sojae, and decreased upon light irradiation
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
involved in the biosynthesis of all acridone alkaloids
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
involved in the biosynthesis of all acridone alkaloids
-
?
N-methylanthraniloyl-CoA + 3 malonyl-CoA
1,3-dihydroxy-N-methylacridone + CoA + CO2
-
-
-
-
?
N-methylanthraniloyl-CoA + 3 malonyl-CoA
1,3-dihydroxy-N-methylacridone + CoA + CO2
-
-
-
-
?
N-methylanthraniloyl-CoA + 3 malonyl-CoA
1,3-dihydroxy-N-methylacridone + CoA + CO2
-
anthraniloyl CoA is not accepted as starter substrate, the anthranilate N-methylation prior to CoA activation is a key step in acridone alkaloid formation, anthranilate N-methyltransferase is a branch-point enzyme of acridone biosynthesis
-
-
?
additional information
?
-
enzyme accepts bulky substrates as starters and carries out one to three condensations to yield various aromatic tetraketides along with some di- and triketides
-
-
?
additional information
?
-
-
enzyme accepts bulky substrates as starters and carries out one to three condensations to yield various aromatic tetraketides along with some di- and triketides
-
-
?
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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
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
-
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
activity is increased upon treatment with crude elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea, syn. Phytophthora sojae, and decreased upon light irradiation
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
activity is increased upon treatment with crude elicitors from the cell wall of Phytophthora megasperma f. sp. glycinea, syn. Phytophthora sojae, and decreased upon light irradiation
-
ir
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
involved in the biosynthesis of all acridone alkaloids
-
?
malonyl-CoA + N-methylanthraniloyl-CoA
CoA + 1,3-dihydroxy-N-methylacridone + CO2
-
involved in the biosynthesis of all acridone alkaloids
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.0043
N-methylanthraniloyl-CoA
product 1,3-dihydroxy-N-methylacridone, pH 7.0, 30Ā°C
0.0374
N-methylanthraniloyl-CoA
product 4-hydroxy-N-methylquinolone, pH 7.0, 30Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
N-methylanthraniloyl-CoA
product 1,3-dihydroxy-N-methylacridone, pH 7.0, 30Ā°C
0.067
N-methylanthraniloyl-CoA
product 4-hydroxy-N-methylquinolone, pH 7.0, 30Ā°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.95
N-methylanthraniloyl-CoA
product 4-hydroxy-N-methylquinolone, pH 7.0, 30Ā°C
5.4
N-methylanthraniloyl-CoA
product 1,3-dihydroxy-N-methylacridone, pH 7.0, 30Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACS2_RUTGR
391
0
42683
Swiss-Prot
other Location (Reliability: 2)
ACS3_RUTGR
391
0
42726
Swiss-Prot
other Location (Reliability: 2)
ACS4_RUTGR
391
0
42710
Swiss-Prot
other Location (Reliability: 2)
U3KRF0_9ROSI
391
0
42830
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
1 * 42000, recombinant enzyme from Escherichia coli, SDS-PAGE and western blot analysis
44000
additional information
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
1 * 42000, recombinant enzyme from Escherichia coli, SDS-PAGE and western blot analysis
dimer
-
2 * 44000-45000, isozyme I and II, analytical ultracentrifugation and SDS-PAGE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S132T/A133S/V265F
-
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
-
site-directed mutagenesis, 75% reduction of ACS catalytic activity, but 2fold increased chalcone synthase activity
additional information
-
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baumert, A.; Maier, W.; Gröger, D.; Deutzmann, R.
Purification and properties of acridone synthase from cell suspension cultures of Ruta graveolens L.
Z. Naturforsch. C
49
26-32
1994
Ruta graveolens
brenda
Maier, W.; Baumert, A.; Schumann, B.; Furukawa, H.; Gröger, D.
Synthesis of 1,3-dihydroxy-N-methylacridone and its conversion to rutacridone by cell-free extracts of Ruta-graveolens cell cultures
Phytochemistry
32
691-698
1993
Ruta graveolens
-
brenda
Lukacin.R.; Springob, K.; Urbanke, C.; Ernwein, C.; Schröder, G.; Schröder, J.; Matern, U.
Native acridone synthases I and II from Ruta graveolens L. form homodimers
FEBS Lett.
448
135-140
1999
Ruta graveolens
brenda
Junghanns, K.T.; Kneusel, R.E.; Groger, D.; Matern, U.
Differential regulation and distribution of acridone synthase in Ruta graveolens
Phytochemistry
49
403-411
1998
Ruta graveolens
brenda
Junghanns, K.T.; Kneusel, R.E.; Baumert, A.; Maier, W.; Groeger, D.; Matern, U.
Molecular cloning and heterologous expression of acridone synthase from elicited Ruta graveolens L. cell suspension cultures
Plant Mol. Biol.
27
681-692
1995
Ruta graveolens (Q9FSC0), Ruta graveolens
brenda
Springob, K.; Lukacin, R.; Ernwein, C.; Groning, I.; Matern, U.
Specificities of functionally expressed chalcone and acridone synthases from Ruta graveolens
Eur. J. Biochem.
267
6552-6559
2000
Ruta graveolens
brenda
Lukacin, R.; Schreiner, S.; Matern, U.
Transformation of acridone synthase to chalcone synthase
FEBS Lett.
508
413-417
2001
Ruta graveolens
brenda
Wanibuchi, K.; Zhang, P.; Abe, T.; Morita, H.; Kohno, T.; Chen, G.; Noguchi, H.; Abe, I.
An acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata
FEBS J.
274
1073-1082
2007
Huperzia serrata (A3E7Z7), Huperzia serrata
brenda
Lukacin, R.; Schreiner, S.; Silber, K.; Matern, U.
Starter substrate specificities of wild-type and mutant polyketide synthases from Rutaceae
Phytochemistry
66
277-284
2005
Ruta graveolens
brenda
Morita, H.; Kondo, S.; Kato, R.; Wanibuchi, K.; Noguchi, H.; Sugio, S.; Abe, I.; Kohno, T.
Crystallization and preliminary crystallographic analysis of an acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata
Acta Crystallogr. Sect. F
63
576-578
2007
Huperzia serrata
brenda
Rohde, B.; Hans, J.; Martens, S.; Baumert, A.; Hunziker, P.; Matern, U.
Anthranilate N-methyltransferase, a branch-point enzyme of acridone biosynthesis
Plant J.
53
541-553
2008
Ruta graveolens
brenda
Mori, T.; Shimokawa, Y.; Matsui, T.; Kinjo, K.; Kato, R.; Noguchi, H.; Sugio, S.; Morita, H.; Abe, I.
Cloning and structure-function analyses of quinolone- and acridone-producing novel type III polyketide synthases from Citrus microcarpa
J. Biol. Chem.
288
28845-28858
2013
Citrus x microcarpa (U3KRF0), Citrus x microcarpa
brenda
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