Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.74 - chalcone synthase and Organism(s) Medicago sativa and UniProt Accession P30074

for references in articles please use BRENDA:EC2.3.1.74
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Medicago sativa
UNIPROT: P30074
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Medicago sativa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
chalcone synthase, ascl1, ascl2, chs-1, chs_h1, gmirchs, flavanone synthase, ripks4, chs-7, 6'-deoxychalcone synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chalcone synthase
-
6'-deoxychalcone synthase
-
-
-
-
chalcone synthase
-
-
-
-
chalcone synthetase
-
-
-
-
CHS
-
-
-
-
DOCS
-
-
-
-
flavanone synthase
-
-
-
-
flavanone synthetase
-
-
-
-
naringenin-chalcone synthase
-
-
-
-
synthase, flavanone
-
-
-
-
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 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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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
-
SUBSTRATE
PRODUCT                       
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
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + 4-coumaroyl-CoA
4 CoA + naringenin chalcone + 3 CO2
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
-
iodoacetic acid
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHS2_MEDSA
389
0
42706
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the crstal structure with PDB ID 1BQ6 for structure-function analysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C164A
-
reduced activity
H303Q
-
reduced activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jez, J.M.; Noel, J.P.
Mechanism of chalcone synthase: pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase
J. Biol. Chem.
275
39640-39646
2000
Medicago sativa
Manually annotated by BRENDA team
Li, D.; Zheng, Q.; Zhang, H.
A quantum mechanics study on the reaction mechanism of chalcone formation from p-coumaroyl-CoA and malonyl-CoA catalyzed by chalcone synthase
Theoret. Chem. Accounts
122
157-166
2009
Medicago sativa (P30074)
-
Manually annotated by BRENDA team