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
2.3.1.74
-
RECOMMENDED NAME
GeneOntology No.
naringenin-chalcone synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
-
-
-
-
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
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
P30074
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6'-deoxychalcone synthase
-
-
-
-
chalcone synthase
-
-
-
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase
P30074
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase
B2NJ30
-
chalcone synthase
A9ZMJ2
-
chalcone synthase
-
-
chalcone synthase
O22122, O48564, Q9LRB2
gene chs
chalcone synthase
C3RTM5
-
chalcone synthase
-
-
chalcone synthase
-
-
chalcone synthase 6
P30080
-
chalcone synthase 7
Q84V87
-
chalcone synthase C2-Idf-I
-
-
chalcone synthase C2-Idf-II
-
-
chalcone synthetase
-
-
-
-
CHS
-
-
-
-
CHS
P30074
-
CHS
B2NJ30
-
CHS
C3RTM5
-
CHS6
P30080
-
CHS7
P30081, Q84V87
-
CHS_H1
-
-
Cs-COR126
-
-
DOCS
-
-
-
-
EC 2.3.1.120
-
-
formerly
-
flavanone synthase
-
-
-
-
flavanone synthetase
-
-
-
-
naringenin-chalcone synthase 6
P30080
-
Q7Y1X9 {SwissProt}
-
-
Q7Y1Y0 {SwissProt}
-
-
RiPKS4
B0LDU5
-
RiPKS5
B0LDU6
-
synthase, flavanone
-
-
-
-
GmIRCHS
Q6X0M8
-
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
CAS REGISTRY NUMBER
COMMENTARY
56803-04-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Col-O, gene CHS
-
-
Manually annotated by BRENDA team
cv. Ruby, gene CsCHS-bo
-
-
Manually annotated by BRENDA team
carrot, ssp. sativa
-
-
Manually annotated by BRENDA team
carrot, var Kurdagosun
-
-
Manually annotated by BRENDA team
two distinct activity peaks during fruit ripening at early and late developmental stages; cv. Elsanta
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
L. Merr. cv RCAT Angora (3150 CHU) and cv Harovinton (3100 CHU)
SwissProt
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
barley, inoculated with fungus blumeria graminis
-
-
Manually annotated by BRENDA team
chs_H1 variant, clone No. 132
SwissProt
Manually annotated by BRENDA team
chs_H1 variant, clone No. 1539
SwissProt
Manually annotated by BRENDA team
chs_H1 variant, clone No. 211
SwissProt
Manually annotated by BRENDA team
-
Q9FUB7
SwissProt
Manually annotated by BRENDA team
Juglans sp.
walnut, Juglans nigra * Juglans regia
-
-
Manually annotated by BRENDA team
white-flowering mutant line 18
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
AB 136, Rio Tibagi, Carioca and Macanudo
-
-
Manually annotated by BRENDA team
Scots pine
-
-
Manually annotated by BRENDA team
MS-Gensuke and Uchiki-Gensuke
SwissProt
Manually annotated by BRENDA team
cultivar: Royalty
SwissProt
Manually annotated by BRENDA team
cv. Royalty, raspberry
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
ringworm bush
-
-
Manually annotated by BRENDA team
Silene sp.
-
-
-
Manually annotated by BRENDA team
white mustard
-
-
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
Verbena sp.
-
-
-
Manually annotated by BRENDA team
cv. Cabernet Sauvigon
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
chalcone synthase the first enzyme in the flavonoid pathway
metabolism
-
chalcone synthase is the key enzyme of flavonoid biosynthesis pathway
metabolism
-
chalcone synthase is involved in the biosynthesis of anthocyanin
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
physiological function
A9ZMJ2
part of flavonoid biosynthetic pathway
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
2 malonyl-CoA + acetyl-CoA
4-hydroxy-6-methyl-2-pyrone + 3 CoA + 2 CO2
show the reaction diagram
-
poor substrate
i.e. triacetic acid lactone
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 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-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
C3RTM5
-
-
-
?
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
P30074
-
-
-
?
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
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
-
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-, Q2VAZ3
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
P30080
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
B0LDU5, B0LDU6
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
first step in flavonoid biosynthesis in plants
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
key enzyme in flavonoid synthesis
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
key enzyme in prenylflavonoid biosynthesis
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
B0LDU5, B0LDU6
RiPKS5 synthesizes naringenin chalcone exclusively
-
-
?
4-coumaroyl-CoA and 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
-
?
5-hydroxyferulyl-CoA + malonyl-CoA
? + CoA + CO2
show the reaction diagram
B0LDU5, B0LDU6
-
-
-
?
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
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
Silene sp.
-
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
B0LDU5, B0LDU6
-
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
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
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
Verbena sp.
-
less efficient than 4-coumaroyl-CoA
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
80% enzyme activity
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
-
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
-
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
B0LDU5, B0LDU6
-
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
-
i.e. pinocembrin
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
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
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
15% of the reaction rate with 4-coumaroyl-CoA
i.e. pinocembrin
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
-
87.5% of the activity with 4-coumaroyl-CoA + malonyl-CoA
-
-
?
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
-
-
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
-
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
B0LDU5, B0LDU6
-
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
-
formation of by-products
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
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
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
80% enzyme activity
-
-
?
ferulyl-CoA + malonyl-CoA
homoeriodictyol + CoA + CO2
show the reaction diagram
-
reaction gives one major and 3 minor reaction products, none of those is identical with homoeriodictyol
-
-
?
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 + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
show the reaction diagram
-
-
-
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
show the reaction diagram
-
-
-
-
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
show the reaction diagram
-
-
the formation of this product requires an additional reductase
?
malonyl CoA + 4-coumaroyl-CoA + NADH
6'-deoxychalcone + CoA + CO2 + NAD+
show the reaction diagram
-
-
the formation of this product requires an additional reductase
?
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
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
Silene sp., Verbena sp.
-
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
byproduct 2.7-4.2% reservatrol
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
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
show the reaction diagram
Juglans sp.
-
-
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
show the reaction diagram
-
-
chalcone is the initial product that spontaneously transforms to naringenin
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
in the presence of NADH liquiritigenin i.e. 5-deoxyflavanone is formed as a byproduct
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
no formation of naringenin
-
-
?
malonyl-CoA + 4-coumaroyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
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
-
-
?
malonyl-CoA + 4-coumaroyl-CoA + NADPH
5'-deoxyflavanone + CoA + CO2 + NADP+
show the reaction diagram
-
-
-
?
malonyl-CoA + 4-coumaroyl-CoA + NADPH
5'-deoxyflavanone + CoA + CO2 + NADP+
show the reaction diagram
-
-
the formation of this product requires an additional reductase
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
-
-
i.e. 2,4,6-trihydroxybenzophenone along with byproducts
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
-
poor substrate at pH 8, most efficient substrate at pH 6.5
-
-
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
-
22.3% of the activity with 4-coumaroyl-CoA + malonyl-CoA
-
-
?
malonyl-CoA + butyryl-CoA
phlorobutyrophenone + CO2 + CoA
show the reaction diagram
-
-
-
?
malonyl-CoA + cinnamoyl-CoA
?
show the reaction diagram
-, Q2VAZ3
62% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + dihydro-p-coumaroyl-CoA
?
show the reaction diagram
-, Q2VAZ3
50% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + dihydrocinnamoyl-CoA
?
show the reaction diagram
-, Q2VAZ3
23% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + hexanoyl-CoA
phlorocaprophenone + CO2 + CoA
show the reaction diagram
-
-
-
?
malonyl-CoA + hexanoyl-CoA
phlorocaprophenone + CO2 + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA + hexanoyl-CoA
?
show the reaction diagram
-, Q2VAZ3
37% of the activity with 4-coumaroyl-CoA
-
-
?
malonyl-CoA + isovaleryl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl-CoA + isovaleryl-CoA
?
show the reaction diagram
-, Q2VAZ3
15% of the activity with 4-coumaroyl-CoA
-
-
?
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
-, Q2VAZ3
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
-
-
?
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
B0LDU5, B0LDU6
-
-
-
?
malonyl-CoA + phenylacetyl-CoA
phlorobenzylketone + CoA + Co2
show the reaction diagram
-
-
i.e. 2,4,6-trihydroxyphenylbenzylketone
?
additional information
?
-
-
enzyme accepts both aromatic and aliphatic CoA esters as starter substrate
-
-
-
additional information
?
-
-
induction of chalcone synthase and phenylalanine ammonia-lyase by salicylic acid and Colletotrichum lindemuthianum
-
-
-
additional information
?
-
-
key enzyme of the flavonoid/anthocyanin biosynthesis pathway
-
-
-
additional information
?
-
-
CHS function is an important regulatory point of substrate flow between the flavonoid and the phenylpropanoid pathways
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q6X0M8
GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
P30074
-
-
-
?
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
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
first step in flavonoid biosynthesis in plants
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
key enzyme in flavonoid synthesis
-
-
?
4-coumaroyl-CoA + malonyl-CoA
naringenin chalcone + CoA + CO2
show the reaction diagram
-
key enzyme in prenylflavonoid biosynthesis
-
-
?
caffeoyl-CoA + 3 malonyl-CoA
eriodictyol + 4 CoA + 3 CO2
show the reaction diagram
-
-
-
?
additional information
?
-
-
induction of chalcone synthase and phenylalanine ammonia-lyase by salicylic acid and Colletotrichum lindemuthianum
-
-
-
additional information
?
-
-
key enzyme of the flavonoid/anthocyanin biosynthesis pathway
-
-
-
additional information
?
-
-
CHS function is an important regulatory point of substrate flow between the flavonoid and the phenylpropanoid pathways
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q6X0M8
GmIRCHS is the I gene that inhibits pigmentation over the entire seed coat, resulting in a uniform yellow color of mature harvested seeds
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CaCl2
Juglans sp.
-
1 mM, 15% increase of activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-methylcyclopropene
Q06FE4
-
2'-hydroxygenistein
-
-
2-mercaptoethanol
-
above 5 mM
2-mercaptoethanol
-
100 mM
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
Juglans sp.
-
substrate inhibition above 0.03 mM
4-Coumaroyl-CoA
-
above 0.01 mM
apigenin
-
50% inhibition at 0.009 mM
apigenin
-
competitive with respect to 4-coumaroyl-CoA and non competitive with respect to malonyl-CoA
Ca2+
-
10-20% decrease at 1 mM
cerulenin
-
50% inhibition at 0.001 mg per assay
cerulenin
-
-
CoA
-
50% inhibition at 0.036 mM
CoA
-
total inhibition at 0.25 mM
CoA
-
50% inhibition at 0.01 mM
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
-
50% inhibition at 0.045 mM
eriodictyol
-
-
eriodictyol chalcone
-
-
ethylene glycol
-
-
iodoacetamide
-
-
iodoacetamide
-
due to labeling of C164
iodoacetic acid
-
-
isoliquiritigenin
-
-
isovitexin 2''-O-arabinoside
-
50% inhibition at 0.062 mM
Kievitone
-
50% inhibition at 0.001 mM
luteolin
-
50% inhibition at 0.013 mM
malonyl-3'-dephospho-CoA
-
50% inhibition at 0.003 mM
malonyl-CoA
Juglans sp.
-
-
malonyl-CoA
-
substrate inhibition above 0.05 mM
Mg2+
-
10-20% decrease at 1 mM
Naringenin
-
50% inhibition at 0.045 mM
Naringenin
-
50% inhibition of naringenin formation and total inhibition of eriodictyol formation
Naringenin
-
total inhibition at 0.4 mM
Naringenin
-
50% inhibition at 0.01 mM
Naringenin
-
0.1 mM
Naringenin chalcone
-
50% inhibition of naringenin formation and total inhibition of eriodictyol formation
Naringenin chalcone
-
-
Naringenin chalcone
-
0.1 mM
p-chloromercuribenzoate
-
50% inhibition at 2.5 mM
potassium ascorbate
-
-
Zn2+
-
50% decrease above 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Juglans sp.
-
activation
2-mercaptoethanol
-
also leads to increased formation of by-products
2-mercaptoethanol
-
2fold increase at 20 mM
2-mercaptoethanol
-
activation
Bovine serum albumin
-
-
-
Bovine serum albumin
-
activation
-
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0006
-
4-Coumaroyl-CoA
-
-
0.0006
-
4-Coumaroyl-CoA
-
-
0.0006
-
4-Coumaroyl-CoA
-
-
0.0008
-
4-Coumaroyl-CoA
-
isozyme AI
0.001
-
4-Coumaroyl-CoA
-
isozyme AII
0.0015
-
4-Coumaroyl-CoA
-
-
0.0016
-
4-Coumaroyl-CoA
Juglans sp.
-
-
0.0017
-
4-Coumaroyl-CoA
-
-
0.002
-
4-Coumaroyl-CoA
-
-
0.0022
-
4-Coumaroyl-CoA
-
-
0.0023
-
4-Coumaroyl-CoA
-
-
0.0023
-
4-Coumaroyl-CoA
-
C169S/Q100E/K180Q triple mutant
0.0025
-
4-Coumaroyl-CoA
-
wild-type enzyme
0.0049
-
4-Coumaroyl-CoA
-
pH 7.0, 35C, wild-type enzyme
0.00517
-
4-Coumaroyl-CoA
-
pH 8.0, 30C
0.0057
-
4-Coumaroyl-CoA
-
-
0.0078
-
4-Coumaroyl-CoA
-
pH 7.0, 35C, mutant enzyme L263M/F265Y/S338G
0.0361
-
4-Coumaroyl-CoA
-
-
0.0409
-
4-Coumaroyl-CoA
-
-
0.0054
-
benzoyl-CoA
-
pH 7.0, 35C, mutant enzyme L263M/F265Y/S338G
0.0068
-
benzoyl-CoA
-
pH 7.0, 35C, wild-type enzyme
0.00145
-
caffeoyl-CoA
-
-
0.0016
-
caffeoyl-CoA
-
-
0.0077
-
caffeoyl-CoA
-
-
0.011
-
Decanoyl-CoA
-
pH 8.0, 30C
0.001
-
Feruloyl-CoA
-
-
0.0025
-
Feruloyl-CoA
-
-
0.0007
-
Hexanoyl-CoA
-
-
0.0245
-
Hexanoyl-CoA
-
pH 8.0, 30C
0.0149
-
isobutyryl-CoA
-
-
0.008
-
isovaleryl-CoA
-
-
0.001
-
malonyl-CoA
-
-
0.0014
0.0015
malonyl-CoA
-
-
0.0019
-
malonyl-CoA
-
isozyme AII
0.002
-
malonyl-CoA
-
isozyme AI
0.0026
-
malonyl-CoA
Juglans sp.
-
-
0.003
-
malonyl-CoA
-
-
0.0063
-
malonyl-CoA
-
-
0.0099
-
malonyl-CoA
-
pH 7.0, 35C, mutant enzyme L263M/F265Y/S338G
0.0108
-
malonyl-CoA
-
pH 7.0, 35C, wild-type enzyme
0.018
-
malonyl-CoA
-
-
0.0214
-
malonyl-CoA
-
-
35
-
malonyl-CoA
-
37C, pH 7.2
0.017
-
NADPH
-
-
0.0122
-
Octanoyl-CoA
-
pH 8.0, 30C
0.048
-
p-Coumaroyl-CoA
-
37C, pH 7.2
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.007
-
4-Coumaroyl-CoA
-
pH 7.0, 35C, mutant enzyme L263M/F265Y/S338G
0.0167
-
4-Coumaroyl-CoA
-
pH 8.0, 30C
0.021
-
4-Coumaroyl-CoA
-
-
0.042
-
4-Coumaroyl-CoA
-
pH 7.0, 35C, wild-type enzyme
0.0113
-
benzoyl-CoA
-
pH 7.0, 35C, wild-type enzyme
0.0156
-
benzoyl-CoA
-
pH 7.0, 35C, mutant enzyme L263M/F265Y/S338G
0.044
-
Decanoyl-CoA
-
pH 8.0, 30C
0.066
-
Octanoyl-CoA
-
pH 8.0, 30C
0.147
-
Hexanoyl-CoA
-
pH 8.0, 30C
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
-
apigenin
-
-
0.0207
-
Kievitone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00083
-
-
-
0.00176
-
-
-
0.0064
-
-
-
0.0085
-
-
-
0.00918
-
-
-
0.0188
-
-
-
0.162
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
caffeoyl-CoA
6.5
7
-
caffeoyl-CoA
6.5
-
-
caffeoyl-CoA
6.5
-
-
caffeoyl-CoA and feruloyl-CoA
6.8
-
Juglans sp.
-
assay at
6.8
-
-
caffeoyl-CoA
7
-
-
substrate 4-coumaroyl-CoA
7.5
-
-
4-coumaroyl-CoA
7.5
-
-
assay at
7.9
-
-
4-coumaroyl-CoA
8
-
Juglans sp.
-
4-coumaroyl-CoA
8
-
-
4-coumaroyl-CoA
8
-
-
4-coumaroyl-CoA
8
-
-
4-coumaroyl-CoA
8
-
-
substrate hexanoyl-CoA
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
Juglans sp.
-
-
45
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-
less than 50% of maximal activity above and below
20
60
-
50% activity at 20C, 50C and 60C
25
45
Juglans sp.
-
less than 40% of maximal activity above and below
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.79
-
O22122, O48564, Q9LRB2
sequence calculation
5.86
-
O22122, O48564, Q9LRB2
sequence calculation; sequence calculation
7.1
-
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
2% activity in pollen, 98% activity in tapetum
Manually annotated by BRENDA team
B2NJ30, -
expression of CHS is strongly inhibited in the later stages of anther development in sterility cytoplasm
Manually annotated by BRENDA team
C3RTM5
devloping, CHSL1 shows a restricted expression pattern and is specific for the anther
Manually annotated by BRENDA team
Juglans sp.
-
-
Manually annotated by BRENDA team
P30081, Q84V87
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
B0LDU5, B0LDU6
the transcripts of RiPKS4 and RiPKS5 accumulate at a lower level during fruit development in comparison to RiPKS1; the transcripts of RiPKS4 and RiPKS5 accumulate at a lower level during fruit development in comparison to RiPKS1
Manually annotated by BRENDA team
Q06FE4
CHS content decreases dramatically during the 1-week ripening period
Manually annotated by BRENDA team
-
grape berry
Manually annotated by BRENDA team
B0LDU5, B0LDU6
;
Manually annotated by BRENDA team
A9ZMJ2
low amount
Manually annotated by BRENDA team
Q45XN8, Q58G81, Q5PU46
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; 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
Manually annotated by BRENDA team
Q45XN8, Q58G81, Q5PU46
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; 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); 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
Manually annotated by BRENDA team
Q58G81
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
Manually annotated by BRENDA team
P30080
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
Manually annotated by BRENDA team
Q45XN8, Q58G81, Q5PU46
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
Manually annotated by BRENDA team
Q58G81
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
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
C3RTM5
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
Q58G81
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
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
a plastid-distributed isozyme, synthesized throughout developmental stages
Manually annotated by BRENDA team
-
of the skin cells
Manually annotated by BRENDA team
-
a vacuole-distributed isozyme synthesized at late developmental stage
Manually annotated by BRENDA team
additional information
-
no activity in chloroplasts
-
Manually annotated by BRENDA team
additional information
-
subcellular localization study
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42800
-
-
calculated from amino acid sequence
43000
-
-
calculated from amino acid sequence
43000
-
-
wild type enzyme migrates at 43000 Da, HvCHS2 migrated at a slightly lower molecular mass
43000
-
-
-
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
77000
-
-
sedimentation equilibrium centrifugation
77000
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
Q58G81
x * 42600, SDS-PAGE
?
O22122, O48564, Q9LRB2
x * 42504, sequence calculation; x * 42589, sequence calculation; x * 42638, sequence calculation
?
C3RTM5
x * 41800, CHSL1, about, sequence determination
dimer
-
2 * 40000-45000, SDS-PAGE
dimer
-
1 * 43000 + 1 * 44000, SDS-PAGE
dimer
-
1 * 78000 + 1 * 88000, non-denaturating PAGE, 1 * 48000 + 1 * 62000, gel filtration
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
additional information
-
the enzyme contains four CHS-specific conserved motifs and a CHS-family signature sequence GFGPG
additional information
O22122, O48564, Q9LRB2
molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview; molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview; molecular structure: secondary structures and homology-based three-dimensional structural modelling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using the crstal structure with PDB ID 1BQ6 for structure-function analysis, overview
P30074
molecular modeling of structure
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
25
-
-
50% inactivation after 90 min
25
-
-
stable up to
100
-
-
boiling for 10 min leads to complete inactivity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
withdrawal of 2-mercaptoethanol after ammonium sulfate precipitation leads to increased stability during further purification
-
0.1% bovine serum albumin stabilizes
Juglans sp.
-
5% activity after freezing for 1 h without presence of glycerol
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to oxygen
Juglans sp.
-
487454
exclusion of oxygen during purification gives improved yield and purity of product
-
487465
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 3 mg protein/ml
-
-70C, decrease of activity in solutions below 1 mg/ml
-
-20C, 10% glycerol, 6 months, 20% loss of activity
-
-70C, 0.1% bovine serum albumin, at least 3 weeks
Juglans sp.
-
-70C, 0.04 mM potassium phosphate buffer, pH 8.0, 14 mM 2-mercaptoethanol, 20% v/v glycerol
-
-70C, 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
-
-20C, 4 mg/ml bovine serum albumin
-
-20C, 0.4 M phosphate buffer, pH 6.5, 20% v/v glycerol, 4 weeks
-
-20C, 30% initial loss of activity, remaining activity stable for 14 d
-
-20C, 5 mg/ml bovine serum albumin, 12 d
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
fusion protein with glutathione S-transferase
-
gene CHS, realtime PCR expression analysis
-
gene CHS and mutant gene CHS-wf, DNA and amino acid sequence determination and analysis, expression analysis by semi-quantitative RT-PCR
-
gene CsCHS-bo, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, cloning and expression in Escherichia coli strain DH5alpha
-
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
-
GCHS2 and GCHS26 with different enzymatic and structural properties
-
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
P30080
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
-
wild type enzyme and HvCHS2 with different substrate requirements
-
expression in Escherichia coi.
-
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
A0AMG7, A0AMG8, A0AMG9
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
Q9FUB7
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
-
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
-
-
Q45XN8, Q58G81, Q5PU46
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
Q58G81
expressed in Escherichia coli
-
expression in Escherichia coli
-
wild type and mutants
-
expression in Escherichia coli JM109
A9ZMJ2
expression in Escherichia coli; expression in Escherichia coli
B0LDU5, B0LDU6
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
O22122, O48564, Q9LRB2
isoforms
-
expression in Escherichia coli, site directed mutagenesis, sequence alignment with EC 2.3.1.95
-
gene CHSL1, DNA and amino acid sequence determination and analysis, pattern of expression, overview
C3RTM5
gene CHS, DNA and amino acid sequence determination and analysis, expression analysis
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
cold-stress treatment, 4C for 24 h
-
decrease at flowering
A9ZMJ2
no change in the expression of CHS gene after leaf wounding treatment, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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
C164A
-
reduced activity
F215S
P30074
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
P30074
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
-
reduced activity
C170R
-
more than 50% decrease in activity with hexanoyl-CoA, increase in thermal stability
C170S
-
more than 80% decrease in activity with hexanoyl-CoA, increase in thermal stability
C164S
-
inhibition by diethyl diphosphate is pH dependent
A133S
-
fully functional enzyme
S132T
-
fully functional enzyme
V265F
-
reduced activity
V265F/S132T/A133S
-
triple mutant, reduced specific activity
S338V
-
mutant CHS produces octaketides from eight molecules of malonyl-CoA
T197G/G256L/S338T
-
high octaketide producing activity
C135A
-
77% enzyme activity
C169A
-
no enzyme activity
C169S
-
no enzyme activity
C169S/Q100E
-
28% of wild-type activity
C169S/Q100E/K180Q
-
15% of wild-type activity
C195A
-
increased enzyme activity
C347A
-
44% enzyme activity
C65A
-
15% enzyme activity
C89A
-
71% enzyme activity
K180Q
-
no enzyme activity
Q100E
-
14% of wild-type activity
S158C
-
90% of wild-type 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
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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