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Information on EC 2.3.1.74 - chalcone synthase
for references in articles please use BRENDA:EC2.3.1.74
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.74 chalcone synthase
IUBMB Comments
The enzyme catalyses the first committed step in the biosynthesis of flavonoids. It can also act on dihydro-4-coumaroyl-CoA, forming phloretin.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.3.1.74
- flavonoid
- anthocyanins
- flower
-
phenylpropanoids
-
ammonia-lyase
- polyketide
-
proneural
- dihydroflavonol
-
neuroendocrine
- anthocyanidin
-
neurogenesis
-
achaete-scute
- elicitors
-
4-reductase
- petunia
- stilbene
-
helix-loop-helix
- colletotrichum
-
phytoalexins
-
cinnamic
-
anthracnose
- hybrida
- petal
-
neurod1
- parsley
-
leucoanthocyanidin
- antirrhinum
-
3\'-hydroxylase
- 3-o-glucosyltransferase
- 4-coumarate
- petroselinum
- gloeosporioides
-
isoflavonoids
- glycinea
- corolla
-
sclcs
-
phox2b
-
acervuli
- pinocembrin
- lupulus
-
g-boxes
- biotechnology
- lindemuthianum
-
r2r3-myb
- crispum
-
4.3.1.5
-
re-isolated
- agriculture
-
elicitor-treated
- fructicola
-
4-coumarate:coa
- cinnamoyl-coa
showSynonyms
chalcone synthase, ascl1, ascl2, chs-1, chs_h1, gmirchs, flavanone synthase, ripks4, 6'-deoxychalcone synthase, malonyl-coa:4-coumaroyl-coa malonyltransferase (cyclizing), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6'-deoxychalcone synthase
-
-
-
-
chalcone synthase
chalcone synthetase
CHS
Chs1
CHS13
Chs2
CHS3
CHS4
CHS5
CHS6
CHS7
Chs8
CHS_H1
DOCS
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-
-
-
EC 2.3.1.120
-
-
formerly
-
flavanone synthase
-
-
-
-
flavanone synthetase
-
-
-
-
naringenin-chalcone synthase
PKS1
bifunctional enzyme with both chalcone synthase and benzalacetone synthase activity
RinPKS1
bifunctional enzyme with both chalcone synthase and benzalacetone synthase activity
synthase, flavanone
-
-
-
-
additional information
chalcone synthase
-
-
-
-
chalcone synthetase
-
-
-
-
CHS
-
-
-
-
naringenin-chalcone synthase
-
-
-
-
additional information
-
the enzyme is a member of the type III polyketide synthase superfamily
additional information
C3RTM5
the enzyme belongs to a small distinct group of type III polyketide synthases that includes angiosperm and gymnosperm orthologs shown to be anther-specific
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
-
-
-
-
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
reaction mechanism analysis by quantum mechanics calculations, overview. In loading step, only a tetrahedral intermediate is located without transition state. His303 acts as a H31 donor, but not a hydrogen bond donor, to stabilize the intermediate formation. In decarboxylation step, the reaction proceeds via a transition state and is sensitive to the environment. In elongation step, a tetrahedral transition state is located, structure-function analysis, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
condensation
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
aromatic polyketides biosynthesis, flavonoid biosynthesis, flavonoid biosynthesis (in equisetum), flavonoid di-C-glucosylation, naringenin biosynthesis (engineered), phloridzin biosynthesis, xanthohumol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
The enzyme catalyses the first committed step in the biosynthesis of flavonoids. It can also act on dihydro-4-coumaroyl-CoA, forming phloretin.
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CAS REGISTRY NUMBER
COMMENTARY
56803-04-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2RS)-methylmalonyl-CoA + n-hexanoyl-CoA
triketide lactone + 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone
Substrates: -
Products: -
Products: -
?
2 malonyl-CoA + 2 stearoyl-CoA
6-heptadecyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxononadecyl)-2H-pyran-2-one + 2 CoA + 2 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-hydroxycinnamoyl-CoA
4 CoA + naringenin chalcone
-
Substrates: the enzyme catalyzes the condensation of 4-hydroxycinnamoyl-CoA and three malonyl-CoA molecules to form the chalcone derivative, naringenin chalcone, which is the first committed step in the phenylpropanoid pathway of plants, leading to the biosynthesis of flavonoids, isoflavonoids, and anthocyanins
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + caffeoyl-CoA
?
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
3 malonyl-CoA + feruloyl-CoA
?
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + ? + 3 CO2
Substrates: 37% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
3 malonyl-CoA + sinapoyl-CoA
?
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA
1-(4-hydroxyphenyl)pent-1-en-3-one
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
4-coumaroyltriacetic acid lactone + 4 CoA + 3 CO2
-
Substrates: -
Products: wild-type enzyme shows low 4-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitutions V196M, T197A, and V196M/T197A causes a shift toward neutrality of the optimum pH for 4-coumaroyltriacetic acid lactone-producing activity. Enhancement of the tetraketide producing activity upon V196M and V196M/T197A substitutions is most markedly observed when 4-coumaroyl-CoA is used as the starter substrate, and only slightly with benzoyl-, caffeoyl- and hexanoyl-CoA
Products: wild-type enzyme shows low 4-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitutions V196M, T197A, and V196M/T197A causes a shift toward neutrality of the optimum pH for 4-coumaroyltriacetic acid lactone-producing activity. Enhancement of the tetraketide producing activity upon V196M and V196M/T197A substitutions is most markedly observed when 4-coumaroyl-CoA is used as the starter substrate, and only slightly with benzoyl-, caffeoyl- and hexanoyl-CoA
?
4-coumaroyl-CoA + N-methylanthraniloyl-CoA
CoA + naringenin + 4-hydroxyl-1-methyl 2(H) quinolone + 1,3-dihydroxy-n-methyl acridone + CO2
-
Substrates: mutant enzymes F215S and F265V use 4-coumaroyl-CoA as well as N-methylanthraniloyl-CoA as substrates to yield active products such as naringenin, 4-hydroxyl-1-methyl 2(H) quinolone, and 1,3-dihydroxy-n-methyl acridone
Products: -
Products: -
?
5-hydroxyferulyl-CoA + malonyl-CoA
? + CoA + CO2
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + 3 methylmalonyl-CoA
CoA + 4-hydroxy-3,5-dimethyl-6-phenyl-pyran-2-one + 4-hydroxy-3,5-dimethyl-6-(1-methyl-2-oxo-2-phenyl-ethyl)-pyran-2-one + CO2
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + malonyl-CoA
?
Substrates: 22% activity compared to 4-coumaroyl-CoA
Products: -
Products: -
?
benzoyl-CoA + methylmalonyl-CoA
4-hydroxy-3,5-dimethyl-6-phenyl-pyran-2-one + 4-hydroxy-3,5-dimethyl-6-(1-methyl-2-oxo-2-phenyl-ethyl)-pyran-2-one + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + malonyl-CoA
?
Substrates: 43% activity compared to 4-coumaroyl-CoA
Products: -
Products: -
?
cinnamoyl diketide-NAC + (2RS)-methylmalonyl-CoA
methylated triketide styrylpyrone + ?
Substrates: -
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
?
Substrates: 81% activity compared to 4-coumaroyl-CoA
Products: -
Products: -
?
decanoyl-CoA + malonyl-CoA
1-(2,4,6-trihydroxyphenyl)-decan-1-one + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
feruloyl-CoA + malonyl-CoA
?
Substrates: 52% activity compared to 4-coumaroyl-CoA
Products: -
Products: -
?
hexanoyl-CoA + 3 methylmalonyl-CoA
CoA + 4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one + CO2
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + malonyl-CoA
phlorocaprophenone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + methylmalonyl-CoA
4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 3-coumaroyl-CoA
? + CO2 + CoA
-
Substrates: 34.4% of the activity with 4-coumaroyl-CoA + malonyl-CoA
Products: -
Products: -
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
? + CO2 + CoA
-
Substrates: 21.8% of the activity with 4-coumaroyl-CoA + malonyl-CoA
Products: -
Products: -
?
malonyl-CoA + 4-fluorocinnamoyl-CoA
fluorinated chalcone + alpha-pyrone + 2 CoA
Substrates: -
Products: -
Products: -
?
malonyl-CoA + acetyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2
Substrates: the reaction is catalyzed by isoform ASCL2 only
Products: -
Products: -
?
malonyl-CoA + benzoyl-CoA
bis-noryangonin + 4-coumaroyl triacetic acid lactone + CoA + CO2
Substrates: -
Products: -
Products: -
?
malonyl-CoA + butyryl-CoA
phlorobutyrophenone + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + caffeoyl-CoA
?
Substrates: -
Products: -
Products: -
?
malonyl-CoA + dihydro-p-coumaroyl-CoA
?
Substrates: 50% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + dihydrocinnamoyl-CoA
?
Substrates: 23% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + feruloyl-CoA
?
Substrates: -
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2
Substrates: -
Products: -
Products: -
?
malonyl-CoA + n-butyryl-CoA
1-(2,4,6-trihydroxyphenyl)-butan-1-one + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + n-butyryl-CoA
?
Substrates: 43% of the activitry with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + octanoyl-CoA
1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2
-
Substrates: poor substrate
Products: -
Products: -
?
malonyl-CoA + octanoyl-CoA
6-heptyl-4-hydroxy-2H-pyran-2-one + CoA + CO2
Substrates: -
Products: -
Products: -
?
malonyl-CoA + phenylacetyl-CoA
phlorobenzylketone + CoA + Co2
-
Substrates: -
Products: i.e. 2,4,6-trihydroxyphenylbenzylketone
Products: i.e. 2,4,6-trihydroxyphenylbenzylketone
?
malonyl-CoA + sinapoyl-CoA
?
Substrates: -
Products: -
Products: -
?
methylmalonyl-CoA + benzoyl-CoA
triketide alpha-pyrone + tetraketide alpha-pyrone
Substrates: -
Products: -
Products: -
?
n-hexanoyl-CoA + butyryl-CoA
phlorobutyrophenone + phlorocaprophenone
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-CoA
1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
sinapyl-CoA + malonyl-CoA
? + CoA + CO2
Substrates: -
Products: -
Products: -
?
2 malonyl-CoA + acetyl-CoA
4-hydroxy-6-methyl-2-pyrone + 3 CoA + 2 CO2
-
Substrates: poor substrate
Products: i.e. triacetic acid lactone
Products: i.e. triacetic acid lactone
?
2 malonyl-CoA + acetyl-CoA
4-hydroxy-6-methyl-2-pyrone + 3 CoA + 2 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: the reaction has highest efficiency with isoform CHS1. 4-coumaroyl-CoA is the best substrate for isoform CHS1
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: 100% activity
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: the enzyme effectively yields naringenin as a dominant product at pH 7.5
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: when incubated with 4-coumaroyl-CoA and malonyl-CoA as substrates at pH 7.5, the enzyme catalyzes the formation of naringeninchalcone as a major product, along with 4-hydroxybenzalacetone. At pH 9.5, the enzyme effectively yields 4-hydroxybenzalacetone as a dominant product, along with naringenin chalcone
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
C3RTM5
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + butyryl-CoA
4 CoA + phlorobutyrophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + butyryl-CoA
4 CoA + phlorobutyrophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + phlorocaprophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + phlorocaprophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + phlorocaprophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: first step in flavonoid biosynthesis in plants
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: key enzyme in flavonoid synthesis
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: key enzyme in prenylflavonoid biosynthesis
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
Substrates: RiPKS5 synthesizes naringenin chalcone exclusively
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: 80% enzyme activity
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: wild type enzyme uses cinnamoyl-CoA and 4-coumaroyl-CoA at comparable rates whereas feruloyl-CoA is a poor substrate, HvCHS2 converts feruloyl-CoA and caffeoyl-CoA at the highest rate whereas cinnamoyl-CoA is a poor substrate
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
Verbena sp.
-
Substrates: less efficient than 4-coumaroyl-CoA
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: 15% of the reaction rate with 4-coumaroyl-CoA
Products: i.e. pinocembrin
Products: i.e. pinocembrin
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: wild type enzyme uses cinnamoyl-CoA and 4-coumaroyl-CoA at comparable rates whereas feruloyl-CoA is a poor substrate, HvCHS2 converts feruloyl-CoA and caffeoyl-CoA at the highest rate whereas cinnamoyl-CoA is a poor substrate
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: 87.5% of the activity with 4-coumaroyl-CoA + malonyl-CoA
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: -
Products: i.e. pinocembrin
Products: i.e. pinocembrin
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
Substrates: -
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: 80% enzyme activity
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: reaction gives one major and 3 minor reaction products, none of those is identical with homoeriodictyol
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: wild type enzyme uses cinnamoyl-CoA and 4-coumaroyl-CoA at comparable rates whereas feruloyl-CoA is a poor substrate, HvCHS2 converts feruloyl-CoA and caffeoyl-CoA at the highest rate whereas cinnamoyl-CoA is a poor substrate
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
Substrates: -
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
-
Substrates: -
Products: formation of by-products
Products: formation of by-products
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
-
Substrates: -
Products: the formation of this product requires an additional reductase
Products: the formation of this product requires an additional reductase
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
-
Substrates: -
Products: -
Products: -
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
-
Substrates: -
Products: -
Products: -
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
-
Substrates: -
Products: -
Products: -
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
-
Substrates: -
Products: the formation of this product requires an additional reductase
Products: the formation of this product requires an additional reductase
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found, the latter cyclizes spontaneously to naringenin
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found, the latter cyclizes spontaneously to naringenin
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: chalcone is the initial product that spontaneously transforms to naringenin
Products: chalcone is the initial product that spontaneously transforms to naringenin
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: no formation of naringenin
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: in the presence of NADH liquiritigenin i.e. 5-deoxyflavanone is formed as a byproduct
Products: in the presence of NADH liquiritigenin i.e. 5-deoxyflavanone is formed as a byproduct
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: wild type enzyme uses cinnamoyl-CoA and 4-coumaroyl-CoA at comparable rates whereas feruloyl-CoA is a poor substrate, HvCHS2 converts feruloyl-CoA and caffeoyl-CoA at the highest rate whereas cinnamoyl-CoA is a poor substrate
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: byproduct 2.7-4.2% reservatrol
Products: byproduct 2.7-4.2% reservatrol
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: PKS1 produces mainly naringenin chalcone as product with small amounts of 4-coumaroyltriacetic acid lactone as byproduct, PKS3 produces mainly 4-coumaroyltriacetic acid lactone and only small amounts of naringenin chalcone
Products: PKS1 produces mainly naringenin chalcone as product with small amounts of 4-coumaroyltriacetic acid lactone as byproduct, PKS3 produces mainly 4-coumaroyltriacetic acid lactone and only small amounts of naringenin chalcone
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found, the latter cyclizes spontaneously to naringenin
Products: due to the presence of isomerase the immediate product naringenin chalcone is not detectable, instead 4,2',4',6'-tetrahydroxychalcone is found, the latter cyclizes spontaneously to naringenin
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
Verbena sp.
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + 4-coumaroyl-CoA + NADPH
5'-deoxyflavanone + CoA + CO2 + NADP+
-
Substrates: -
Products: the formation of this product requires an additional reductase
Products: the formation of this product requires an additional reductase
?
malonyl-CoA + 4-coumaroyl-CoA + NADPH
5'-deoxyflavanone + CoA + CO2 + NADP+
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + acetyl-CoA
?
-
Substrates: the reaction has highest efficiency with isoform CHS2
Products: -
Products: -
?
malonyl-CoA + acetyl-CoA
?
Substrates: isoform CHS1 exhibits 21.15% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + acetyl-CoA
?
Substrates: isoform CHS2 exhibits 138.11% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
-
Substrates: 22.3% of the activity with 4-coumaroyl-CoA + malonyl-CoA
Products: -
Products: -
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
-
Substrates: poor substrate at pH 8, most efficient substrate at pH 6.5
Products: -
Products: -
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
-
Substrates: -
Products: i.e. 2,4,6-trihydroxybenzophenone along with byproducts
Products: i.e. 2,4,6-trihydroxybenzophenone along with byproducts
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + butyryl-CoA
?
-
Substrates: the reaction has highest efficiency with isoform CHS2
Products: -
Products: -
?
malonyl-CoA + butyryl-CoA
?
Substrates: isoform CHS1 exhibits 18.85% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + butyryl-CoA
?
Substrates: isoform CHS2 exhibits 45.38% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + cinnamoyl-CoA
?
Substrates: 62% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
?
-
Substrates: the reaction has highest efficiency with isoform CHS2. Hexanoyl-CoA is the best substrate for isoform CHS2
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
?
Substrates: 37% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
?
Substrates: isoform CHS1 exhibits 3.09% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
?
Substrates: isoform CHS2 exhibits 2.36% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
phlorocaprophenone + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + hexanoyl-CoA
phlorocaprophenone + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + isovaleryl-CoA
?
Substrates: 15% of the activity with 4-coumaroyl-CoA
Products: -
Products: -
?
malonyl-CoA + octanoyl-CoA
?
-
Substrates: the reaction has highest efficiency with isoform CHS2
Products: -
Products: -
?
malonyl-CoA + octanoyl-CoA
?
Substrates: isoform CHS1 exhibits 22.04% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
malonyl-CoA + octanoyl-CoA
?
Substrates: isoform CHS2 exhibits 72.39% activity compared to 4-coumaryl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-coumaroyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: CHS function is an important regulatory point of substrate flow between the flavonoid and the phenylpropanoid pathways
Products: -
Products: -
?
additional information
?
-
Substrates: neither isoform GASCL1 nor isoform GASCL2 accept 4-coumaroyl-CoA or benzoyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: neither isoform GASCL1 nor isoform GASCL2 accept 4-coumaroyl-CoA or benzoyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
Products: -
Products: -
?
additional information
?
-
-
Substrates: GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
Products: -
Products: -
?
additional information
?
-
Substrates: under the assay conditions, the enzyme exclusively catalyzes the production of naringenin chalcone and CTAL3 from 3 malonyl-CoA and 4-coumaroyl-CoA. In the presence of at least 1 mM CoA, the enzyme almost exclusively produces CTAL
Products: -
Products: -
-
additional information
?
-
-
Substrates: key enzyme of the flavonoid/anthocyanin biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild type enzyme does not accept N-methylanthraniloyl-CoA as substrate
Products: -
Products: -
-
additional information
?
-
Substrates: both chalcone isomerase and chalcone isomerase-lile protein physically interact with the enzyme in a non-competitive manner
Products: -
Products: -
-
additional information
?
-
-
Substrates: induction of chalcone synthase and phenylalanine ammonia-lyase by salicylic acid and Colletotrichum lindemuthianum
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not accept isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not accept isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: 4-coumaroyl-CoA and feruloyl-CoA are the only cinnamoyl-CoA derivatives accepted as starter substrates. RinPKS1 does not accept isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: 4-coumaroyl-CoA and feruloyl-CoA are the only cinnamoyl-CoA derivatives accepted as starter substrates. RinPKS1 does not accept isobutyryl-CoA, isovaleryl-CoA or acetyl-CoA as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme accepts both aromatic and aliphatic CoA esters as starter substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme accepts CoA esters of long-chain fatty acids (up to C12 ester) as substrates, leading to the formation of tetraketide phloroglucinols, triketide, and tetraketide alpha-pyrones. The enzyme accepts diketide-N-acetylcysteamine with less efficiency but cinnamoyl-N-acetylcysteamine as efficiently as cinnamoyl-CoA. The enzyme accepts methylmalonyl-CoA as the extension unit to afford an unnatural C-6-C-5 aromatic polyketide, 1-(4-hydroxyphenyl)-pent-1-en-3-one as a major product along with the bis-noryangonin-type and the 4-coumaroyltriacetic acid lactone-type pyrone by-products, with sequential decarboxylative condensation of 4-coumaroyl-CoA. The enzyme also accepts 4-coumaroyl-CoA analogs in which the 4-hydroxyl group is substituted by halogen (F, Cl, and Br) or a methoxy group as the starter substrate
Products: -
Products: -
-
additional information
?
-
-
Substrates: succinyl-CoA is not accepted as a substrate
Products: -
Products: -
-
additional information
?
-
-
Substrates: homozygous C2-Idf plants show no pigmentation. This allele also inhibits expression of functional C2 alleles in heterozygotes, producing a less pigmented condition instead of the normal deeply pigmented phenotype. The inhibitory effect of C2-Idf occurs through RNA silencing
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + 4-hydroxycinnamoyl-CoA
4 CoA + naringenin chalcone
-
Substrates: the enzyme catalyzes the condensation of 4-hydroxycinnamoyl-CoA and three malonyl-CoA molecules to form the chalcone derivative, naringenin chalcone, which is the first committed step in the phenylpropanoid pathway of plants, leading to the biosynthesis of flavonoids, isoflavonoids, and anthocyanins
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
Products: -
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-cinnamoyl-CoA
4 CoA + pinocembrin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: 100% activity
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: first step in flavonoid biosynthesis in plants
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: key enzyme in flavonoid synthesis
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: key enzyme in prenylflavonoid biosynthesis
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: CHS function is an important regulatory point of substrate flow between the flavonoid and the phenylpropanoid pathways
Products: -
Products: -
?
additional information
?
-
Substrates: GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
Products: -
Products: -
?
additional information
?
-
-
Substrates: GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme of the flavonoid/anthocyanin biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: induction of chalcone synthase and phenylalanine ammonia-lyase by salicylic acid and Colletotrichum lindemuthianum
Products: -
Products: -
?
additional information
?
-
-
Substrates: homozygous C2-Idf plants show no pigmentation. This allele also inhibits expression of functional C2 alleles in heterozygotes, producing a less pigmented condition instead of the normal deeply pigmented phenotype. The inhibitory effect of C2-Idf occurs through RNA silencing
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-Nucleotidase
-
i.e. EC 3.1.3.6 hydrolyzes the phosphate group in the 3'-position of adenosine, a part of the CoA thioester substrates
-
diethyl diphosphate
-
inhibition of wild-type enzyme is pH independent, inhibition of C164S mutant increases with increasing pH between pH 6.2 to pH 7.4
apigenin
-
competitive with respect to 4-coumaroyl-CoA and non competitive with respect to malonyl-CoA
CoA
in the presence of at least 1 mM CoA, the enzyme almost exclusively produces CTAL and amost no THC
naringenin
-
50% inhibition of naringenin formation and total inhibition of eriodictyol formation
naringenin chalcone
-
50% inhibition of naringenin formation and total inhibition of eriodictyol formation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
type IV chalcone isomerase-like protein (CHIL) binds to the enzyme to serve as a rectifier - rather than an activator - of promiscuous enzyme; it enhances enzyme-catalyzed THC production and diminishes CTAL formation without enhancing total polyketide production, thereby facilitating the efficient influx of substrates from the general phenylpropanoid pathway to the flavonoid pathway
-
additional information
-
type IV chalcone isomerase-like protein (CHIL) binds to the enzyme to serve as a rectifier - rather than an activator - of promiscuous enzyme; it enhances enzyme-catalyzed THC production and diminishes CTAL formation without enhancing total polyketide production, thereby facilitating the efficient influx of substrates from the general phenylpropanoid pathway to the flavonoid pathway
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001303
4-coumaroyl-CoA
pH and temperature not specified in the publication
0.001121
4-coumaroyl-CoA
in the presence of chalcone isomerase and chalcone isomerase-like protein, pH and temperature not specified in the publication
0.001321
4-coumaroyl-CoA
in the presence of chalcone isomerase-like protein, pH and temperature not specified in the publication
0.001545
4-coumaroyl-CoA
in the presence of chalcone isomerase, pH and temperature not specified in the publication
0.00333
4-coumaroyl-CoA
mutant enzyme K55A, pH and temperature not specified in the publication
0.00473
4-coumaroyl-CoA
-
in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.00771
4-coumaroyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.012
4-coumaroyl-CoA
mutant enzyme K268A, pH and temperature not specified in the publication
0.0136
4-coumaroyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.0142
4-coumaroyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
0.0198
4-coumaroyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.0213
4-coumaroyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
0.0497
4-coumaroyl-CoA
-
in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.0308
malonyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.0374
malonyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
0.0397
malonyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.0579
malonyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00695
4-coumaroyl-CoA
pH and temperature not specified in the publication
0.05
4-coumaroyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
0.0505
4-coumaroyl-CoA
in the presence of chalcone isomerase-like protein, pH and temperature not specified in the publication
0.0517
4-coumaroyl-CoA
mutant enzyme K268A, pH and temperature not specified in the publication
0.0617
4-coumaroyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.085
4-coumaroyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.087
4-coumaroyl-CoA
-
in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.109
4-coumaroyl-CoA
mutant enzyme K55A, pH and temperature not specified in the publication
0.11
4-coumaroyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.175
4-coumaroyl-CoA
in the presence of chalcone isomerase, pH and temperature not specified in the publication
0.178
4-coumaroyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
1.27
4-coumaroyl-CoA
-
in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
3.04
4-coumaroyl-CoA
in the presence of chalcone isomerase and chalcone isomerase-like protein, pH and temperature not specified in the publication
0.038
malonyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
0.055
malonyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
0.063
malonyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
0.082
malonyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.14
malonyl-CoA
-
in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
0.59
malonyl-CoA
-
in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
4-coumaroyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
4.29
4-coumaroyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
4.3
4-coumaroyl-CoA
mutant enzyme K268A, pH and temperature not specified in the publication
8
4-coumaroyl-CoA
wild type enzyme, pH and temperature not specified in the publication
8.21
4-coumaroyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
12.56
4-coumaroyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
18.5
4-coumaroyl-CoA
-
in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
20
4-coumaroyl-CoA
mutant enzyme R58A, pH and temperature not specified in the publication
25.7
4-coumaroyl-CoA
-
in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C
33
4-coumaroyl-CoA
mutant enzyme K55A, pH and temperature not specified in the publication
38.2
4-coumaroyl-CoA
in the presence of chalcone isomerase-like protein, pH and temperature not specified in the publication
53.3
4-coumaroyl-CoA
pH and temperature not specified in the publication
113.3
4-coumaroyl-CoA
in the presence of chalcone isomerase, pH and temperature not specified in the publication
170
4-coumaroyl-CoA
isoform CHS2, pH and temperature not specified in the publication
787
4-coumaroyl-CoA
isoform CHS1, pH and temperature not specified in the publication
2711
4-coumaroyl-CoA
in the presence of chalcone isomerase and chalcone isomerase-like protein, pH and temperature not specified in the publication
50
acetyl-CoA
isoform CHS1, pH and temperature not specified in the publication
1240
acetyl-CoA
isoform CHS2, pH and temperature not specified in the publication
50
butyryl-CoA
isoform CHS1, pH and temperature not specified in the publication
990
butyryl-CoA
isoform CHS2, pH and temperature not specified in the publication
10
hexanoyl-CoA
isoform CHS1, pH and temperature not specified in the publication
300
hexanoyl-CoA
isoform CHS2, pH and temperature not specified in the publication
0.66
malonyl-CoA
mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication
1.39
malonyl-CoA
mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication
1.69
malonyl-CoA
mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication
2.65
malonyl-CoA
wild type enzyme, at pH 8.0, temperature not specified in the publication
30
octanoyl-CoA
isoform CHS1, pH and temperature not specified in the publication
580
octanoyl-CoA
isoform CHS2, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
about 50% activity at 30°C, about 90% activity at 40°C, 100% activity at 50°C, about 70% activity at 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
6.1
6.2
6.3
6.6
isoform CHS088, calculated from amino acid sequence
6.8
isoform CHS768, calculated from amino acid sequence
6.9
6.1
isoform CHS2, calculated from amino acid sequence
6.2
isoform CHS1, calculated from amino acid sequence
6.3
isoform CHS3, calculated from amino acid sequence
6.9
isoform CHS444, calculated from amino acid sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. AC Barrie, AABBDD, chalcone synthase-like gene CHSL1
C3RTM5
UniProt
brenda
two distinct activity peaks during fruit ripening at early and late developmental stages; cv. Elsanta
-
-
brenda
L. Merr. cv RCAT Angora (3150 CHU) and cv Harovinton (3100 CHU)
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highest expression. The enzyme is primarily localized in the growth point, leaf primordium, and young leaves of leaf buds
brenda
C3RTM5
expression of CHSL1 only within the tapetum during the free and early vacuolated microspore stages in both wheat and triticale
brenda
additional information
highest expression in tapetal cells of the anther
brenda
expression of CHS is strongly inhibited in the later stages of anther development in sterility cytoplasm
brenda
C3RTM5
devloping, CHSL1 shows a restricted expression pattern and is specific for the anther
brenda
expression patterns is higher at 70 d after pollination in both the cultivars. Expression of the gene coincides with the onset of accumulation of isoflavonoids in the embryos. CHS8 is expressed at significantly greater level in RCAT Angora than in Harovinton
brenda
expression patterns is higher at 70 d after pollination in both the cultivars. Expression of the gene coincides with the onset of accumulation of isoflavonoids in the embryos. CHS7 is expressed at significantly greater level in RCAT Angora than in Harovinton
brenda
expression shows significant correlation to the accumulation patterns of anthocyanin during flower development
brenda
CHS content decreases dramatically during the 1-week ripening period
brenda
the transcripts of RiPKS4 and RiPKS5 accumulate at a lower level during fruit development in comparison to RiPKS1
brenda
-
the enzyme is primarily localized in exocarp and vascular bundles of the fruit during berry development
brenda
-
the enzyme is primarily localized in palisade, spongy tissues and vascular bundles of the leaves
brenda
specially expressed in floral organs. Pchs isexpressed both in pigmented flower tissues, including petal, lip, and sepal, at early developmental stages and in colorless reproductive tissue at a late stage
brenda
Phchs5 is the most abundantly expressed chs gene in floral organs and it is specifically transcribed in petal and lip at the stages when anthocyanin accumulates
brenda
Cchs3 is expressed at much lower levels than phchs5. Phchs3 is expressed in pigmented tissue (including lip, petal and sepal) at middle stages (stages 24) and in colorless reproductive tissue at late stage
brenda
specially expressed in floral organs. Pchs isexpressed both in pigmented flower tissues, including petal, lip, and sepal, at early developmental stages and in colorless reproductive tissue at a late stage
brenda
Phchs5 is the most abundantly expressed chs gene in floral organs and it is specifically transcribed in petal and lip at the stages when anthocyanin accumulates
brenda
Cchs3 is expressed at much lower levels than phchs5. Phchs3 is expressed in pigmented tissue (including lip, petal and sepal) at middle stages (stages 24) and in colorless reproductive tissue at late stage
brenda
phchs4 is expressed at much lower levels than phchs5. Phchs4 is only expressed in petal at earlier stages (stage 1-3) and in lip at middle stage (stage 4)
brenda
roughly equivalently expressed in cyanic and acyanic areas except for at stage II and V of flower development
brenda
hairy roots, transformed with the soybean chalcone synthase (CHS6) or isoflavone synthase (IFS2) genes, with dramatically decreased capacity to synthesize isoflavones are produced to determine what effects these changes would have on susceptibility to a fungal pathogen. Blockage of isoflavone synthesis by constitutive expression of two key genes in the isoflavonoid pathway, chalcone synthase and isoflavone synthase leads to the inability to synthesize glyceollin in soybean hairy roots on root resistance to Fusarium solani f. sp. glycines
brenda
-
the enzyme is primarily localized in the endoderm and primary phloem of roots
brenda
specially expressed in floral organs. Pchs isexpressed both in pigmented flower tissues, including petal, lip, and sepal, at early developmental stages and in colorless reproductive tissue at a late stage
brenda
Cchs3 is expressed at much lower levels than phchs5. Phchs3 is expressed in pigmented tissue (including lip, petal and sepal) at middle stages (stages 24) and in colorless reproductive tissue at late stage
brenda
-
patterns of enzyme gene expression in different genotypes of shoots undergoing rhizogenesis are associated with observed flavonoids content, and a high frequency of rhizogenesis is accompanied with low flavonoid content in shoots
brenda
-
the enzyme is primarily localized in primary phloem and pith ray in the stems
brenda
additional information
-
wild-type and mutant expression anaylsis in plant tissues, overview
brenda
additional information
no expression in stem, stamen, pistil, leaf and shuck
brenda
additional information
no expression in stem, stamen, pistil, leaf and shuck
brenda
additional information
no expression in stem, stamen, pistil, leaf and shuck
brenda
additional information
-
no expression in stem, stamen, pistil, leaf and shuck
brenda
additional information
transcripts of CHS1 are detected in all examined samples at different expression levels
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
a plastid-distributed isozyme, synthesized throughout developmental stages
brenda
-
a vacuole-distributed isozyme synthesized at late developmental stage
brenda
additional information
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica. The results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants
metabolism
physiological function
metabolism
-
chalcone synthase is involved in the biosynthesis of anthocyanin
metabolism
-
chalcone synthase is the key enzyme of flavonoid biosynthesis pathway
metabolism
-
chalcone synthase is an entrance enzyme of flavonoid metabolism and a critical point to regulation of biosynthesis of different flavonoid compounds that directly contribute to color and monthfeel of grape and wine
metabolism
the enzyme is involved in anthocyanin biosynthesis
metabolism
the enzyme participates in sporopollenin biosynthesis and exine formation within the locule
metabolism
the enzyme catalyzes the initial step of the phenylpropanoid pathway
metabolism
isoform CHS1 is a key component of the isoflavonoid metabolon, a protein complex to enhance efficiency of isoflavonoid production
metabolism
-
the enzyme catalyzes the rate-limiting step of (2S)-naringenin (the essential flavonoid skeleton) biosynthesis
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
metabolism
-
rate-limiting enzyme in the biosynthesis of chalcone as well as the subsequent flavonoids
physiological function
-
chalcone synthase is the first enzyme in flavonoid biosynthesis pathway, and is responsible for establishing the C15 skeleton of flavonoid compounds as well as being correlated with anthocyanin synthesis in several plants
physiological function
-
chalcone synthase is involved in control of flavonoid biosynthesis and in promoting rhizogenesis in walnut microshoots
physiological function
chalcone synthase expression in flowers shows significant correlation to the accumulation patterns of anthocyanin during flower development. Its ectopic overexpression in Arabidopsis thaliana tt4 mutants fully restors the pigmentation phenotype of the seed coats, cotyledons and hypocotyls, while transgenic Petunia hybrida expressing CHS1 shows flower color alteration from white to pink
physiological function
ectopic expression of CHS in Marchantia paleacea callus raises the content of the total flavonoids
physiological function
the enzyme plays an important role in biosynthesis of flavonoids
physiological function
-
isoforms CHS13, CHS8 and CHS21 from can significantly enhance the anthocyanin accumulation and up-regulate the expression of flavonoid biosynthetic structural genes in blueberry leaves and apple fruits
physiological function
-
isoform CHS24 acts as the main chalcone isomerase isozyme and both isoforms CHS24 and CHS8 redundantly contribute to the UV-induced production of sakuranetin in rice leaves
Show AA Sequence and Transmembrane Helices (2828 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42800
43000
48000
-
isozyme AI, gel filtration, differences in MW may be due to different spatial conformations of AI and AII
62000
77000
78000
-
isozyme AII, non-denaturing gel electrophoresis, differences in MW may be due to different spatial conformations of AI and AII
88000
-
isozyme AI, non-denaturing gel electrophoresis, differences in MW may be due to different spatial conformations of AI and AII
additional information
-
comparison of amino acid sequence with resveratrol synthase, EC 2.3.1.95
43000
-
wild type enzyme migrates at 43000 Da, HvCHS2 migrated at a slightly lower molecular mass
62000
-
isozyme AII, gel filtration, differences in MW may be due to different spatial conformations of AI and AII
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
x * 42800, isoform CHS3, calculated from amino acid sequence
?
x * 43400, isoform CHS1, calculated from amino acid sequence
?
x * 43600, isoform CHS2, calculated from amino acid sequence
?
x * 42590, isoform CHS3, calculated from amino acid sequence
?
x * 43090, isoform CHS1, calculated from amino acid sequence
?
x * 42640, isoform CHS2, calculated from amino acid sequence
?
-
x * 43400, isoform CHS24, calculated from amino acid sequence
?
x * 42101, isoform CHS768, calculated from amino acid sequence
?
x * 42742, isoform CHS088, calculated from amino acid sequence
?
x * 45314, isoform CHS444, calculated from amino acid sequence
dimer
-
1 * 78000 + 1 * 88000, non-denaturating PAGE, 1 * 48000 + 1 * 62000, gel filtration
homodimer
2 * about 43230, calculated from amino acid sequence
additional information
-
the enzyme contains four CHS-specific conserved motifs and a CHS-family signature sequence GFGPG
additional information
molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview
additional information
molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview
additional information
molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ubiquitination
Kelch domain-containing F-box protein physically interacts with the enzyme and specifically mediates its ubiquitination and degradation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using 30% (w/v) PEG 4000, 0.2 M ammonium acetate and 0.1 M sodium citrate (pH 5.6)
hanging-drop vapor-diffusion method using buffered protein solutions (10-15 mg/ml) mixed with equal volumes of the reservoir solution and incubated at 4°C. Crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica
hanging-drop vapor-diffusion method, incubation at 4°C. Crystal structures of biphenyl synthase from Malusx02domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase: chalcone synthase from Malus domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions
using the crstal structure with PDB ID 1BQ6 for structure-function analysis, overview
hanging drop vapor diffusion method, using 0.2 M sodium formate and 20% (v/v) PEG 3350 with 10 molar excesses of naringenin and CoA
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T197A
-
mutation caused no substantial enhancement of the p-coumaroyltriacetic acid lactone-producing activity
V196M
-
mutant produces non-chalcone product p-coumaroyltriacetic acid lactone from p-coumaroyl-CoA and malonyl-CoA. Mutation results in a loss of tetrahydroxychalcone-producing activity, as well as a 12.6fold enhancement of p-coumaroyltriacetic acid lactone-producing activity at pH 7.5. Wild-type enzyme shows low p-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitution V196M causes a shift toward neutrality of the optimum pH for p-coumaroyltriacetic acid lactone-producing activity
V196M/T197A
-
mutant produces significant amounts of non-chalcone product p-coumaroyltriacetic acid lactone from p-coumaroyl-CoA and malonyl-CoA, along with a small amount of 2',4,4',6'-tetrahydroxychalcone. Wild-type enzyme shows low p-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitution V196M/T197A causes a shift toward neutrality of the optimum pH for p-coumaroyltriacetic acid lactone-producing activity
F215S
F265V
K268A
the mutation results in an enhanced naringenin chalcone/4-coumaroyltriacetic acid lactone production ratio. The catalytic efficiency of the mutant is 54% of that observed in the wild type enzyme
K55A
the mutant exhibits greater catalytic efficiency for total tetraketide production compared to the wild type, with increase of 4.1fold
R68A
the mutant exhibits greater catalytic efficiency for total tetraketide production compared to the wild type, with increase of 2.5fold
F265Y
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 7.2:1 for the mutant enzyme
F265Y/S338G
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 2.2:1 for the mutant enzyme
G256A
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 4.0:1 for the mutant enzyme
G256A/L263M/F265Y
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 12.5:1 for the mutant enzyme
G256A/L263M/F265Y/S338G
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 1.1:1 for the mutant enzyme
G256A/S338G
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 3.0:1 for the mutant enzyme
L263M
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 4.0:1 for the mutant enzyme
L263M/F265Y
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 3.7:1 for the mutant enzyme
L263M/F265Y/S338G
-
mutant enzyme preferres benzoyl-CoA over 4-coumaroyl-CoA,relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 1.0:1.9 for the mutant enzyme
L263M/S338G
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 3.9:1 for the mutant enzyme
S338G
-
relative activity with 4-coumaroyl-CoA and benzoyl-CoA as starter substrate is 4.5:1 for wild-type enzyme and 4.4:1 for the mutant enzyme
R72S
-
mutant chalcone synthase in white-flowering line 18, mutant enzyme has no detectable activity
F215S
F215Y
the mutation does not significantly alter the Kd for CoA or acetyl-CoA binding, but dramatically alters the turnover rates for malonyl-CoA decarboxylation compared to the wild-type enzyme
G256A
-
with 4-coumaroyl-CoA as a starter molecule, the mutant produces notably more tetraketide lactone than the wild type enzyme
G256F
-
the mutation causes an increase in the levels of styrylpyrone bis-noryangonin from a triketide intermediate
G256L
-
the mutation causes an increase in the levels of styrylpyrone bis-noryangonin from a triketide intermediate
G256V
-
with 4-coumaroyl-CoA as a starter molecule, the mutant produces notably more tetraketide lactone than the wild type enzyme
T197L/G256L/S338I
-
the mutant is functionally identical to 2-pyrone synthase, and produces tyrosine ammonia lyase from acetyl-CoA and two molecules of malonyl-CoA
C170R
C170S
C198F
Q82P
Q82P/C198F
R105Q
G256L
-
the mutation causes a dramatic increase in the octaketide-forming activity of the enzyme
S338T
-
the mutation causes a dramatic increase in the octaketide-forming activity of the enzyme
S338V
T197G
-
the mutation causes a dramatic increase in the octaketide-forming activity of the enzyme
A308K
-
the mutant shows 1.63fold improved activity compared to the wild type enzyme. The mutant has reduced catalytic efficiency (kcat/Km) toward 4-coumaroyl-CoA, but significantly increased catalytic efficiency toward malonyl-CoA
A380R
-
the mutant shows 1.21fold improved activity compared to the wild type enzyme. The mutant has reduced catalytic efficiency (kcat/Km) toward 4-coumaroyl-CoA, but significantly increased catalytic efficiency toward malonyl-CoA
E61K
-
the mutant shows 1.34fold improved activity compared to the wild type enzyme. The mutant has reduced catalytic efficiency (kcat/Km) toward 4-coumaroyl-CoA, but significantly increased catalytic efficiency toward malonyl-CoA
S208C
-
the mutant shows 1.22fold improved activity compared to the wild type enzyme. The mutant has reduced catalytic efficiency (kcat/Km) toward 4-coumaroyl-CoA, but significantly increased catalytic efficiency toward malonyl-CoA
S208N
-
the mutant shows 2.34fold improved activity compared to the wild type enzyme. The mutant has reduced catalytic efficiency (kcat/Km) toward 4-coumaroyl-CoA, but significantly increased catalytic efficiency toward malonyl-CoA
E183K
the mutation causes almost complete protein aggregation of chalcone synthase 2 with reduced pigmentation in maize
additional information
F215S
functionally active mutant that prefers N-methylanthraniloyl-CoA over p-coumaroyl-CoA. Analyses of tobacco leaves transiently expressing mutant genes show high levels of naringenin, acridones and quinolone derivatives compared to wild-type enzyme
F215S
-
the mutant uses 4-coumaroyl-CoA as well as N-methylanthraniloyl-CoA as substrates to yield active products such as naringenin, 4-hydroxyl-1-methyl 2(H) quinolone, and 1,3-dihydroxy-n-methyl acridone
F265V
functionally active mutant that prefers N-methylanthraniloyl-CoA over p-coumaroyl-CoA. Analyses of tobacco leaves transiently expressing mutant genes show high levels of naringenin, acridones and quinolone derivatives compared to wild-type enzyme
F265V
-
the mutant uses 4-coumaroyl-CoA as well as N-methylanthraniloyl-CoA as substrates to yield active products such as naringenin, 4-hydroxyl-1-methyl 2(H) quinolone, and 1,3-dihydroxy-n-methyl acridone
F215S
the mutation does not significantly alter the Kd for CoA or acetyl-CoA binding, but dramatically alters the turnover rates for malonyl-CoA decarboxylation compared to the wild-type enzyme
F215S
-
the mutant preferentially accepts N-methylanthraniloyl-CoA, which cannot be used by wild type enzyme, to generate N-methylanthraniloyltriacetic acid lactone
C170R
more than 50% decrease in activity with hexanoyl-CoA, increase in thermal stability
C170R
-
the mutation causes a decrease in the ability of the enzyme to use hexanoyl-CoA as a starter molecule, which directly affected the production of pyrone derivatives (products)
C170S
more than 80% decrease in activity with hexanoyl-CoA, increase in thermal stability
C170S
-
the mutation causes a decrease in the ability of the enzyme to use hexanoyl-CoA as a starter molecule, which directly affected the production of pyrone derivatives (products)
Q82P
the mutant exhibits reduced chalcone-forming activity because its Km value with 4-coumaroyl-CoA as the starter substrate is about 2times higher than that of the wild type enzyme. Additionally, the mutant loses 4-hydroxybenzalacetone-forming activity at pH 7.0-9.0
Q82P
-
the mutation causes a change in the pH dependence activity and the product profile of the enzyme
Q82P/C198F
the mutant exhibits benzalacetone synthase activity. The catalytic efficiencies of the mutant for 4-coumaroyl-CoA and malonyl-CoA are lower than that of wild type enzyme
Q82P/C198F
-
the double mutant is able to save the complete loss of enzyme activity caused by the C198F single mutation
R105Q
the mutant exhibits benzalacetone synthase activity. The catalytic efficiency of the mutant for 4-coumaroyl-CoA is higher than that of wild type enzyme
R105Q
-
the mutation causes a change in the pH dependence activity and the product profile of the enzyme
S338V
-
mutant CHS produces octaketides from eight molecules of malonyl-CoA
S338V
-
the mutant produces octaketides SEK4/SEK4b from eight molecules of malonyl-CoA
additional information
-
construction of transgenic Arabidosis thaliana plants expressing four different viral suppressor proteins, i.e. the p38 protein of Turnip Crinkle Virus, the p25 protein of Potato Virus X, the 2b proteins of Cucumber Mosaic Virus and Tomato Aspermy Virus, using transfection with Agrobacterium tumefaciens, in the plants purple anthocyanins pigments accumulate to very high levels in the rosette leaves and stem during plant development, phenotypes, overview
additional information
-
isolation of a naturally occuring mutant gene CHS-wf with two mutations in BcCHS-wf, both with A to G transitions, one at position +37 bp and the other at +970 bp. Both nucleotide substitutions occur in AGA codes for arginine into GGA for glycin at residue +13 and into AGC coding for serine at residue +229, respectively, resulting in a white-flower phenotype
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
half-life 3 h in 1.4 mM 2-mercaptoethanol, increase of stability with 14 mM 2-mercaptoethanol
25
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
withdrawal of 2-mercaptoethanol after ammonium sulfate precipitation leads to increased stability during further purification
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exclusion of oxygen during purification gives improved yield and purity of product
-
487465
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30% initial loss of activity, remaining activity stable for 14 d
-
-70°C, 0.04 mM potassium phosphate buffer, pH 8.0, 14 mM 2-mercaptoethanol, 20% v/v glycerol
-
-70°C, no loss of activity in 0.1 M imidazole-HCl buffer, pH 6.8, 20 mM sodium ascorbate, 10% v/v glycerol for several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homogeneity
Ni-NTA column chromatography
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
an octaploid (Fragaria x ananassa cv. Calypso) genotype of strawberry is transformed with an antisense chalcone synthase (CHS) gene construct using a ripening related CHS cDNA from Fragaria x ananassa cv. Elsanta under the control of the constitutive CaMV 35S promoter via Agrobacterium tumefaciens. Out of 25 transgenic lines, nine lines showed a reduction in CHS mRNA accumulation of more than 50% as compared to the untransformed cv. Calypso control
-
expressed in Arabidopsis thaliana mesophyll protoplasts
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli JM109 cells and in leaves of Arabidopsis thaliana
expressed in Escherichia coli Rosetta-gami (DE3) and BL21-Rosetta (DE3) cells
expressed in Escherichia coli strain BL21(DE3) and Saccharomyces cerevisiae strain HB26
-
expressed in Escherichia coli, Arabidopsis thaliana tt4 mutants and Nicotiana tabacum
-
expression in Escherichia coli
expression in Escherichia coli, site directed mutagenesis, sequence alignment with EC 2.3.1.95
-
expression of the coding sequence of Pchs in Nicotiana tabacum can lead to darker flower limbs than seen in controls, and some transgenic plants exhibited abnormality in growth of pollen tubes
GCHS2 and GCHS26 with different enzymatic and structural properties
-
gene CHS and mutant gene CHS-wf, DNA and amino acid sequence determination and analysis, expression analysis by semi-quantitative RT-PCR
-
gene CHS, DNA and amino acid sequence determination and analysis, expression analysis
-
gene CHS-A, DNA and amino acid sequence determination and analysis, molecular phylogram analysis of SbCHS family and CHS families from other plants, phylogenetic tree
gene CHS-B, DNA and amino acid sequence determination and analysis, molecular phylogram analysis of SbCHS family and CHS families from other plants, phylogenetic tree
gene CHS-C, DNA and amino acid sequence determination and analysis, molecular phylogram analysis of SbCHS family and CHS families from other plants, phylogenetic tree
gene CHSL1, DNA and amino acid sequence determination and analysis, pattern of expression, overview
C3RTM5
gene CsCHS-bo, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, cloning and expression in Escherichia coli strain DH5alpha
-
hairy roots, transformed with the soybean chalcone synthase (CHS6) or isoflavone synthase (IFS2) genes, with dramatically decreased capacity to synthesize isoflavones are produced to determine what effects these changes would have on susceptibility to a fungal pathogen
infiltration of Nicotiana benthamiana leaves with chs_H1 promoter/GUS chimeras leads to a 24.8-fold increase of the GUS activity when coinfiltrated with the pap1 gene. Coinfiltration of the native chs_H1 gene with pap1 leads to an increased accumulation of chs_H1 mRNA. Transgenic lines of Petunia hybrida expressing the pap1 gene showed unusual patterns of UV-A-inducible pigmentation and anthocyanin accumulation in parenchymatic and medulla cells. Infiltration of transgenic leaves of Petunia hybrida with chs_H1 and pap1 genes arranged as a tandem led to quick pigmentation within 12 h after UV-A irradiation
introduction of the phenylpropanoid pathway with the genes for phenylalanine ammonia lyase (PAL) from Rhodosporidium toruloides, 4-coumarate:coenzyme A (CoA) ligase (4CL) from Arabidopsis thaliana, and chalcone synthase (CHS) from Hypericum androsaemum into two Saccharomyces cerevisiae strains, namely, AH22 and a pad1 knockout mutant. Each gene is cloned and inserted into an expression vector under the control of a separate individual GAL10 promoter
isoforms CHS13, CHS8 and CHS21 are expressed in Malus domestica fruits
-
isolation and characterization of cDNA sequences encoding yellow lupin chalcone synthase. Chalcone synthase is encoded by at least two genes. The two sequences may have evolved by gene duplication
overexpression in Escherichia coli as glutathione-S-transferase fusion protein, wild-type and mutant enzymes: L263M, F265Y, G256A, S338G, L263M/F265Y, G256A/S338G, L263M/S338G, F265Y/S338G, L263M/F265Y/S338G, G256A/L263M/F265Y, G256A/L263M/F265Y/S338G
-
recombinant Escherichia coli cells containing four genes for a phenylalanine ammonia-lyase, cinnamate/coumarate:CoA ligase, chalcone synthase, and chalcone isomerase, in addition to the acetyl-CoA carboxylase, have been established for efficient production of (2S)-naringenin from tyrosine and (2S)-pinocembrin from phenylalanine. Further introduction of the flavone synthase I gene from Petroselinum crispum under the control of the T7 promoter and the synthetic ribosome-binding sequence in pACYCDuet-1 causes the Escherichia coli cells to produce flavones: apigenin (13 mg/l) from tyrosine and chrysin (9.4 mg/l) from phenylalanine
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5alpha cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ability and effectiveness of four different viral suppressor proteins, i.e. the p38 protein of Turnip Crinkle Virus, the p25 protein of Potato Virus X, the 2b proteins of Cucumber Mosaic Virus and Tomato Aspermy Virus, that interfere with posttranscriptional gene silencing of the endogenous chalcone synthase gene in Arabidopsis thaliana when the silencing trigger and the viral suppressor protein are expressed from the same transgene locus. The silencing trigger consists of an inverted-repeat transgene construct that induces PTGS of the endogenous Arabidopsis thaliana CHS gene with high efficiency, overview
-
after 3.5-7 days of UV-B irradiation, the accumulation of enzyme transcript is higher in the treated group compared to non-irradiated plants
enzyme expression is induced in response to Verticillium dahliae infection
ethylene affects negatively the enzyme expression. Visible light treatment causes a significant reduction in enzyme expression after 3 days
-
increase in transcript level of PgF3H with respect to the growth of the fruits
increased gene expression upon treatment with methyl jasmonate, salcylic acid and abscisisc acid
isoform CHS4 is up-regulated under 38°C but shows little change at 45°C in peel
-
isoform CHS8 expression is markedly increased in the chs24 mutant under UV stress conditions compared to that in the wild type
-
isoforms CHS5, CHS6 and CHS7 are continuously down-regulated under 38°C and 45°C treatment
-
nitric oxide is responsible for the up-regulation of the enzyme expression during wound stress. Relative expression of the enzyme increases by 2fold in wounded plants upon treatment with nitric oxide and jasmonic acid
-
no change in the expression of CHS gene after leaf wounding treatment, overview
-
overexpression of the nuclear-localized protein MOS9 results in a reduction of enzyme transcript levels
the enzyme expression increases gradually with the development of fruit
the enzyme expression level gradually increases with flower development and reaches a maximum at the early flowering stage
-
the enzyme expression of isoform CHS06 is decreased in response to salicylic acid treatment
-
the enzyme expression of isoforms CHS01, CHS02, CHS03, CHS05, CHS07, CHS08, CHS12, CHS13 and CHS14 is increased in response to salicylic acid treatment
-
the expression profile of isoform CHS1 increases steadily in the early two stages, decreases in the following two stages, and achieves its highest expression level in the last stage of flower development
-
the maximum accumulation of the enzyme protein and gene transcript in berry skins occurs at early stage (20 days after full bloom)
-
the mRNA expression of isoform CHS088 is decreased about 0.6fold by cold treatment (4°C for 3 h) or NaCl treatment (200 mM for 6 h). The mRNA expression of isoform CHS088 is decreased about 0.75fold by abscisic acid treatment (0.05 mM for 1 h)
the mRNA expression of isoform CHS088 is increased about 2.5fold by UV exposure for 6 h
the mRNA expression of isoform CHS088 is not influenced by 20% (w/v) polyethylene glycol or 0.05 mM methyl jasmonate treatment
the mRNA expression of isoform CHS444 is decreased about 0.3fold by cold treatment (4°C for 3 h) or 0.5fold by NaCl treatment (200 mM for 6 h). The mRNA expression of isoform CHS444 is decreased about 0.75fold by abscisic acid treatment (0.05 mM for 1 h)
the mRNA expression of isoform CHS444 is increased about 3fold by UV exposure for 6 h. The mRNA expression of isoform CHS444 is increased about 1.5fold by 20% (w/v) polyethylene glycol treatment for 6 h. The mRNA expression of isoform CHS444 is increased about 3.5fold by 0.05 mM methyl jasmonate treatment for 1 h
the mRNA expression of isoform CHS768 is decreased about 0.6fold by cold treatment (4°C for 3 h) or NaCl treatment (200 mM for 6 h)
the mRNA expression of isoform CHS768 is increased about 3.5fold by UV exposure for 6 h. The mRNA expression of isoform CHS768 is increased about 2.5fold by 20% (w/v) polyethylene glycol treatment for 6 h
the mRNA expression of isoform CHS768 is not influenced by abscisic acid treatment (0.05 mM for 1 h)
treatment with 6-benzylaminopurine increases enzyme expression around day 5 during postharvest storage. The enzyme expression is strongly increased by modified atmospheres and slightly by heat treatment. UV-C radiation increases the expression of the enzyme after 3 days
-
upon infection with hop stunt viroid, expression of chalcone synthase decreases up to 40fold with concomittant decrease in the expression of HlbHLH2 and an increase in the expression of HlMyb3 encoding transcription factors that form a ternary complex with WDR1 for CHS_H1 promoter activation
enzyme expression is induced in response to Verticillium dahliae infection
-
enzyme expression is induced in response to Verticillium dahliae infection
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
upon infection with hop stunt viroid, expression of chalcone synthase decreases up to 40fold with concomittant decrease in the expression of HlbHLH2 and an increase in the expression of HlMyb3 encoding transcription factors that form a ternary complex with WDR1 for CHS_H1 promoter activation
biotechnology
-
Agrobacterium-mediated infection of Petunia hybrida plants with tobacco rattle virus bearing fragments of Petunia genes results in systemic infection and virus-induced gene silencing of the homologous host genes. Infection with TRV containing a chalcone synthase fragment results in silencing of anthocyanin production in infected flowers. Value of virus-induced gene silencing with tandem constructs containing CHS as reporter and a target gene as a tool for examining the function of floral-associated genes
EXTERNAL LINKS (specific for EC-Number 2.3.1.74)
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Release 2026.1 (March 2026)
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