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2.3.1.74: chalcone synthase

This is an abbreviated version!
For detailed information about chalcone synthase, go to the full flat file.

Word Map on EC 2.3.1.74

Reaction

3 malonyl-CoA +

4-coumaroyl-CoA
= 4 CoA +
naringenin chalcone
 + 3 CO2

Synonyms

6'-deoxychalcone synthase, anther-specific chalcone synthase-like enzyme, ASCL1, ASCL2, chalcone synthase, chalcone synthase 6, chalcone synthase 7, chalcone synthase C2-Idf-I, chalcone synthase C2-Idf-II, chalcone synthetase, CHS, CHS var 2, chs-1, CHS-7, CHS01, CHS02, CHS03, CHS04, CHS05, CHS06, CHS07, CHS08, CHS088, CHS09, Chs1, CHS10, CHS11, CHS12, CHS13, CHS14, Chs2, CHS2 chalcone synthase, CHS3, CHS4, CHS444, CHS5, CHS6, CHS7, CHS768, CHS_H1, Cs-COR126, DOCS, EC 2.3.1.120, flavanone synthase, flavanone synthetase, GmIRCHS, MdCHS2, More, naringenin-chalcone synthase, naringenin-chalcone synthase 6, PgCHS, PKS1, Q7Y1Y0, RinPKS1, RiPKS4, RiPKS5, synthase, flavanone, vsad1

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.74 chalcone synthase

Engineering

Engineering on EC 2.3.1.74 - chalcone synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T197A
-
mutation caused no substantial enhancement of the p-coumaroyltriacetic acid lactone-producing activity
V196M
-
mutant produces non-chalcone product p-coumaroyltriacetic acid lactone from p-coumaroyl-CoA and malonyl-CoA. Mutation results in a loss of tetrahydroxychalcone-producing activity, as well as a 12.6fold enhancement of p-coumaroyltriacetic acid lactone-producing activity at pH 7.5. Wild-type enzyme shows low p-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitution V196M causes a shift toward neutrality of the optimum pH for p-coumaroyltriacetic acid lactone-producing activity
V196M/T197A
-
mutant produces significant amounts of non-chalcone product p-coumaroyltriacetic acid lactone from p-coumaroyl-CoA and malonyl-CoA, along with a small amount of 2',4,4',6'-tetrahydroxychalcone. Wild-type enzyme shows low p-coumaroyltriacetic acid lactone-producing activity at pH 7.5, but an appreciable level at pH 10. Substitution V196M/T197A causes a shift toward neutrality of the optimum pH for p-coumaroyltriacetic acid lactone-producing activity
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
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
-
reduced activity
F215S
functionally active mutant that prefers N-methylanthraniloyl-CoA over p-coumaroyl-CoA. Analyses of tobacco leaves transiently expressing mutant genes show high levels of naringenin, acridones and quinolone derivatives compared to wild-type enzyme
F265V
functionally active mutant that prefers N-methylanthraniloyl-CoA over p-coumaroyl-CoA. Analyses of tobacco leaves transiently expressing mutant genes show high levels of naringenin, acridones and quinolone derivatives compared to wild-type enzyme
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
C198F
the mutant almost completely loses the enzyme activity
Q82P
the mutant exhibits reduced chalcone-forming activity because its Km value with 4-coumaroyl-CoA as the starter substrate is about 2times higher than that of the wild type enzyme. Additionally, the mutant loses 4-hydroxybenzalacetone-forming activity at pH 7.0-9.0
Q82P/C198F
the mutant exhibits benzalacetone synthase activity. The catalytic efficiencies of the mutant for 4-coumaroyl-CoA and malonyl-CoA are lower than that of wild type enzyme
R105Q
the mutant exhibits benzalacetone synthase activity. The catalytic efficiency of the mutant for 4-coumaroyl-CoA is higher than that of wild type enzyme
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
additional information