Information on EC 2.3.1.74 - naringenin-chalcone synthase

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The expected taxonomic range for this enzyme is: Embryophyta

EC NUMBER
COMMENTARY hide
2.3.1.74
-
RECOMMENDED NAME
GeneOntology No.
naringenin-chalcone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aromatic polyketides biosynthesis
-
-
Biosynthesis of secondary metabolites
-
-
flavonoid biosynthesis
-
-
Flavonoid biosynthesis
-
-
flavonoid biosynthesis (in equisetum)
-
-
Metabolic pathways
-
-
naringenin biosynthesis (engineered)
-
-
xanthohumol biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
In the presence of NADH and a reductase, 6'-deoxychalcone is produced.
CAS REGISTRY NUMBER
COMMENTARY hide
56803-04-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
oat
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Ruby, gene CsCHS-bo
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
buckwheat
-
-
Manually annotated by BRENDA team
var. Regina
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
barley, inoculated with fungus blumeria graminis
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Juglans sp.
walnut, Juglans nigra * Juglans regia
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
white-flowering mutant line 18
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Scots pine
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
MS-Gensuke and ‘Uchiki-Gensuke
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ringworm bush
-
-
Manually annotated by BRENDA team
Silene sp.
-
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
genotype alpine and prairie
-
-
Manually annotated by BRENDA team
cv. AC Barrie, AABBDD, chalcone synthase-like gene CHSL1
UniProt
Manually annotated by BRENDA team
cv. Apeldoorn
-
-
Manually annotated by BRENDA team
Verbena sp.
-
-
-
Manually annotated by BRENDA team
cv. Cabernet Sauvigon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 malonyl-CoA + acetyl-CoA
4-hydroxy-6-methyl-2-pyrone + 3 CoA + 2 CO2
show the reaction diagram
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
3 malonyl-CoA + 4-hydroxycinnamoyl-CoA
4 CoA + naringenin chalcone
show the reaction diagram
-
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
-
-
?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + ? + 3 CO2
show the reaction diagram
-
37% of the activity with 4-coumaroyl-CoA
-
-
?
4-coumaroyl-CoA + malonyl-CoA
4-coumaroyltriacetic acid lactone
show the reaction diagram
-
-
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 + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
5-hydroxyferulyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
decanoyl-CoA + malonyl-CoA
1-(2,4,6-trihydroxyphenyl)-decan-1-one + CoA + CO2
show the reaction diagram
-
-
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
hexanoyl-CoA + malonyl-CoA
phlorocaprophenone + CoA + CO2
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + methylmalonyl-CoA
4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one + CoA + CO2
show the reaction diagram
-
-
-
-
?
isobutyryl-CoA + malonyl-CoA
?
show the reaction diagram
-
-
-
-
?
isovaleryl-CoA + malonyl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
show the reaction diagram
malonyl-CoA + 3-coumaroyl-CoA
? + CO2 + CoA
show the reaction diagram
-
34.4% of the activity with 4-coumaroyl-CoA + malonyl-CoA
-
-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
? + CO2 + CoA
show the reaction diagram
-
21.8% of the activity with 4-coumaroyl-CoA + malonyl-CoA
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
malonyl-CoA + 4-coumaroyl-CoA + NADPH
5'-deoxyflavanone + CoA + CO2 + NADP+
show the reaction diagram
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
malonyl-CoA + butyryl-CoA
phlorobutyrophenone + CO2 + CoA
show the reaction diagram
-
-
-
?
malonyl-CoA + cinnamoyl-CoA
?
show the reaction diagram
62% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + dihydro-p-coumaroyl-CoA
?
show the reaction diagram
50% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + dihydrocinnamoyl-CoA
?
show the reaction diagram
23% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + hexanoyl-CoA
?
show the reaction diagram
37% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + hexanoyl-CoA
phlorocaprophenone + CO2 + CoA
show the reaction diagram
malonyl-CoA + isovaleryl-CoA
?
show the reaction diagram
malonyl-CoA + n-butyryl-CoA
1-(2,4,6-trihydroxyphenyl)-butan-1-one + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + n-butyryl-CoA
?
show the reaction diagram
43% of the activitry with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + octanoyl-CoA
1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2
show the reaction diagram
-
poor substrate
-
-
?
malonyl-CoA + phenylacetyl-CoA
phlorobenzylketone + CoA + Co2
show the reaction diagram
-
-
i.e. 2,4,6-trihydroxyphenylbenzylketone
?
octanoyl-CoA + malonyl-CoA
1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2
show the reaction diagram
-
-
-
-
?
sinapyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
3 malonyl-CoA + 4-hydroxycinnamoyl-CoA
4 CoA + naringenin chalcone
show the reaction diagram
-
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
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
Juglans sp.
-
1 mM, 15% increase of activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methylcyclopropene
-
2'-hydroxygenistein
-
-
2-mercaptoethanol
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
-
4-Coumaroyl-CoA
apigenin
Ca2+
-
10-20% decrease at 1 mM
cerulenin
Cu2+
-
50% decrease above 1 mM
Dalbergioidin
-
-
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
dithiothreitol
-
60% inhibition
eriodictyol
eriodictyol chalcone
-
-
ethylene glycol
-
-
glycerol
-
-
iodoacetamide
iodoacetic acid
-
-
isoliquiritigenin
-
-
isovitexin 2''-O-arabinoside
-
50% inhibition at 0.062 mM
Kievitone
luteolin
malonyl-3'-dephospho-CoA
-
50% inhibition at 0.003 mM
malonyl-CoA
Mg2+
-
10-20% decrease at 1 mM
naringenin
naringenin chalcone
p-chloromercuribenzoate
-
50% inhibition at 2.5 mM
potassium ascorbate
-
-
Zn2+
-
50% decrease above 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
bovine serum albumin
chlorogenic acid
-
increases eriodictyol formation by 20%
cysteine
Juglans sp.
-
dependent on
dithiothreitol
-
4fold increase at 20 mM
Dowex
Juglans sp.
-
77% increase of activity
-
EDTA
Juglans sp.
-
50 mM, 9% increase of activity
N2
Juglans sp.
-
79% increase of activity
Polyethyleneglycol
Juglans sp.
-
activity strongly dependent on 1.5%
Polyvinylpyrrolidone
Juglans sp.
-
10% w/v essential
Sucrose
Juglans sp.
-
25% increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006 - 0.0409
4-Coumaroyl-CoA
0.0054 - 0.0068
benzoyl-CoA
0.00145 - 0.0077
caffeoyl-CoA
0.011
decanoyl-CoA
-
pH 8.0, 30°C
0.001 - 0.0025
Feruloyl-CoA
0.0007 - 0.0245
Hexanoyl-CoA
0.0149
isobutyryl-CoA
-
-
0.008
isovaleryl-CoA
-
-
0.001 - 35
malonyl-CoA
0.017
NADPH
-
-
0.0122
Octanoyl-CoA
-
pH 8.0, 30°C
0.048
p-Coumaroyl-CoA
-
37°C, pH 7.2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.042
4-Coumaroyl-CoA
0.0113 - 0.0156
benzoyl-CoA
0.044
decanoyl-CoA
Scutellaria baicalensis
-
pH 8.0, 30°C
0.147
Hexanoyl-CoA
Scutellaria baicalensis
-
pH 8.0, 30°C
0.066
Octanoyl-CoA
Scutellaria baicalensis
-
pH 8.0, 30°C
additional information
additional information
Medicago sativa
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
apigenin
-
-
0.0207
Kievitone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0064
-
-
0.0085
-
-
0.00918
-
-
0.0188
-
-
0.162
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
caffeoyl-CoA
6.5
-
caffeoyl-CoA
6.5 - 7
-
caffeoyl-CoA
6.5
-
caffeoyl-CoA and feruloyl-CoA
7
-
substrate 4-coumaroyl-CoA
7.9
-
4-coumaroyl-CoA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
Juglans sp.
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
less than 50% of maximal activity above and below
20 - 60
-
50% activity at 20°C, 50°C and 60°C
25 - 45
Juglans sp.
-
less than 40% of maximal activity above and below
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.79
sequence calculation
5.86
sequence calculation; sequence calculation
7.1
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Juglans sp.
-
-
Manually annotated by BRENDA team
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; 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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
expression of CHSL1 only within the tapetum during the free and early vacuolated microspore stages in both wheat and triticale
Manually annotated by BRENDA team
additional information
-
wild-type and mutant expression anaylsis in plant tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
a plastid-distributed isozyme, synthesized throughout developmental stages
Manually annotated by BRENDA team
-
a vacuole-distributed isozyme synthesized at late developmental stage
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Oryza sativa subsp. indica
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42800
-
calculated from amino acid sequence
48000
-
isozyme AI, gel filtration, differences in MW may be due to different spatial conformations of AI and AII
55000
-
gel filtration, gradient centrifugation
62000
-
isozyme AII, gel filtration, differences in MW may be due to different spatial conformations of AI and AII
69000
-
fusion protein with glutathione S-transferase, SDS-PAGE
75000
-
gel filtration
78000
-
isozyme AII, non-denaturing gel electrophoresis, differences in MW may be due to different spatial conformations of AI and AII
80000 - 85000
-
gel filtration, PAGE under non-denaturing conditions
83000
-
gel filtration
88000
-
isozyme AI, non-denaturing gel electrophoresis, differences in MW may be due to different spatial conformations of AI and AII
120000
-
gel filtration
additional information
-
comparison of amino acid sequence with resveratrol synthase, EC 2.3.1.95
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using the crstal structure with PDB ID 1BQ6 for structure-function analysis, overview
molecular modeling of structure
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
half-life 3 h in 1.4 mM 2-mercaptoethanol, increase of stability with 14 mM 2-mercaptoethanol
4
-
half-life 4-5 d, partially purified enzyme
100
-
boiling for 10 min leads to complete inactivity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1% bovine serum albumin stabilizes
Juglans sp.
-
5% activity after freezing for 1 h without presence of glycerol
-
withdrawal of 2-mercaptoethanol after ammonium sulfate precipitation leads to increased stability during further purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exclusion of oxygen during purification gives improved yield and purity of product
-
487465
sensitive to oxygen
Juglans sp.
-
487454
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.4 M phosphate buffer, pH 6.5, 20% v/v glycerol, 4 weeks
-
-20°C, 10% glycerol, 6 months, 20% loss of activity
-
-20°C, 3 mg protein/ml
-
-20°C, 30% initial loss of activity, remaining activity stable for 14 d
-
-20°C, 4 mg/ml bovine serum albumin
-
-20°C, 5 mg/ml bovine serum albumin, 12 d
-
-70°C, 0.04 mM potassium phosphate buffer, pH 8.0, 14 mM 2-mercaptoethanol, 20% v/v glycerol
-
-70°C, 0.1% bovine serum albumin, at least 3 weeks
Juglans sp.
-
-70°C, decrease of activity in solutions below 1 mg/ml
-
-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
-
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 Escherichia coli
-
expression in Escherichia coi.
-
expression in Escherichia coli
-
expression in Escherichia coli JM109
expression in Escherichia coli, site directed mutagenesis, sequence alignment with EC 2.3.1.95
-
expression in Escherichia coli; expression in Escherichia coli
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
fusion protein with glutathione S-transferase
-
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, realtime PCR 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
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; 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; 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
-
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
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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
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wild type and mutants
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wild type enzyme and HvCHS2 with different substrate requirements
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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
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cold-stress treatment, 4°C for 24 h
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decrease at flowering
no change in the expression of CHS gene after leaf wounding treatment, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T197A
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mutation caused no substantial enhancement of the p-coumaroyltriacetic acid lactone-producing activity
V196M
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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
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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
F265Y
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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mutant chalcone synthase in white-flowering line 18, mutant enzyme has no detectable activity
C164A
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reduced activity
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
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
H303Q
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reduced activity
C170R
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more than 50% decrease in activity with hexanoyl-CoA, increase in thermal stability
C170S
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more than 80% decrease in activity with hexanoyl-CoA, increase in thermal stability
C164S
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inhibition by diethyl diphosphate is pH dependent
A133S
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fully functional enzyme
S132T
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fully functional enzyme
V265F
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reduced activity
V265F/S132T/A133S
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triple mutant, reduced specific activity
S338V
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mutant CHS produces octaketides from eight molecules of malonyl-CoA
T197G/G256L/S338T
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high octaketide producing activity
C135A
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77% enzyme activity
C169A
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no enzyme activity
C169S
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no enzyme activity
C169S/Q100E
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28% of wild-type activity
C169S/Q100E/K180Q
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15% of wild-type activity
C195A
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increased enzyme activity
C347A
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44% enzyme activity
C65A
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15% enzyme activity
C89A
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71% enzyme activity
K180Q
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no enzyme activity
Q100E
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14% of wild-type activity
S158C
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90% of wild-type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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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
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