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Information on EC 2.3.1.159 - acridone synthase and Organism(s) Ruta graveolens and UniProt Accession Q9FSC0

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.159 acridone synthase
IUBMB Comments
Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis)
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This record set is specific for:
Ruta graveolens
UNIPROT: Q9FSC0
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Word Map
The taxonomic range for the selected organisms is: Ruta graveolens
The enzyme appears in selected viruses and cellular organisms
Synonyms
acridone synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acridone synthase
-
-
synthatase, acridone (9Cl)
-
-
-
-
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
condensation
-
Acyl group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
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
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 + 3 malonyl-CoA
1,3-dihydroxy-N-methylacridone + CoA + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
0.5 mM: 95% inhibition
N-ethylmaleimide
-
1 mM: 100% inhibition
p-chloromercuribenzoate
-
0.5 mM: 95% inhibition
additional information
-
light irradiation decreases activity
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.0328
malonyl-CoA
0.0106 - 0.077
N-methylanthraniloyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.18
-
crude extract
14.16
-
purified recombinant isozyme II
6.035
-
purified enzyme
9.54
-
purified recombinant isozyme I
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
isozyme II
7.5
-
isozyme I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
isozyme II, assay range
6 - 9
-
isozyme I, assay range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
isozyme II
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
endodermis and vascular tissue, mRNA and protein
Manually annotated by BRENDA team
-
adjacent to the rhizodermis, mRNA and protein
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACS2_RUTGR
391
0
42683
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
1 * 42000, recombinant enzyme from Escherichia coli, SDS-PAGE and western blot analysis
44000
recombinant enzyme from E. coli, gel filtration
40000
-
2 * 40000, SDS-PAGE
44000
-
isozyme I, gel filtration
45000
-
about, isozyme II, gel filtration
69000
-
gel filtration
81000
-
isozyme I, analytical ultracentrifugation
82000
-
isozyme II, analytical ultracentrifugation
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 42000, recombinant enzyme from Escherichia coli, SDS-PAGE and western blot analysis
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70Ā°C, partially purified, stable for at least 4 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 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 M15
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expression of wild-type and mutants in Escherichia coli
-
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lukacin, R.; Schreiner, S.; Matern, U.
Transformation of acridone synthase to chalcone synthase
FEBS Lett.
508
413-417
2001
Ruta graveolens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team