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Information on EC 2.3.1.74 - chalcone synthase and Organism(s) Hypericum androsaemum and UniProt Accession Q9FUB7

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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.
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This record set is specific for:
Hypericum androsaemum
UNIPROT: Q9FUB7
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Word Map
The taxonomic range for the selected organisms is: Hypericum androsaemum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
chalcone synthase, ascl1, ascl2, chs-1, chs_h1, gmirchs, flavanone synthase, ripks4, malonyl-coa:4-coumaroyl-coa malonyltransferase (cyclizing), chs-7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6'-deoxychalcone synthase
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-
-
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chalcone synthase
chalcone synthetase
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-
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CHS
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-
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DOCS
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-
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flavanone synthase
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flavanone synthetase
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naringenin-chalcone synthase
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synthase, flavanone
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
56803-04-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + 3 malonyl-CoA
naringenin chalcone + 4 CoA + 3 CO2
show the reaction diagram
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-
-
-
?
cinnamoyl-CoA + malonyl-CoA
5,7-dihydroxyflavanone + CoA + CO2
show the reaction diagram
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87.5% of the activity with 4-coumaroyl-CoA + malonyl-CoA
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-
?
malonyl-CoA + 3-coumaroyl-CoA
? + CO2 + CoA
show the reaction diagram
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34.4% of the activity with 4-coumaroyl-CoA + malonyl-CoA
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-
?
malonyl-CoA + 3-hydroxybenzoyl-CoA
? + CO2 + CoA
show the reaction diagram
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21.8% of the activity with 4-coumaroyl-CoA + malonyl-CoA
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-
?
malonyl-CoA + benzoyl-CoA
phlorobenzophenone + CO2 + CoA
show the reaction diagram
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22.3% of the activity with 4-coumaroyl-CoA + malonyl-CoA
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049 - 0.0078
4-coumaroyl-CoA
0.0054 - 0.0068
benzoyl-CoA
0.0099 - 0.0108
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.042
4-coumaroyl-CoA
0.0113 - 0.0156
benzoyl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHSY_HYPAN
390
0
42713
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, B.; Falkenstein-Paul, H.; Schmidt, W.; Beerhues, L.
Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases
Plant J.
34
847-855
2003
Hypericum androsaemum
Manually annotated by BRENDA team
Jiang, H.; Wood, K.V.; Morgan, J.A.
Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae
Appl. Environ. Microbiol.
71
2962-2969
2005
Hypericum androsaemum (Q9FUB7), Hypericum androsaemum
Manually annotated by BRENDA team