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2.3.1.216: 5,7-dihydroxy-2-methylchromone synthase

This is an abbreviated version!
For detailed information about 5,7-dihydroxy-2-methylchromone synthase, go to the full flat file.

Word Map on EC 2.3.1.216

Reaction

5 malonyl-CoA = 5 CoA +

5,7-dihydroxy-2-methyl-4H-chromen-4-one
+ 5 CO2 +
H2O

Synonyms

PCS, pentaketide chromone synthase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.216 5,7-dihydroxy-2-methylchromone synthase

Engineering

Engineering on EC 2.3.1.216 - 5,7-dihydroxy-2-methylchromone synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F80A/Y82A/M207G
-
site-directed mutagenesis, the total cavity volume of the F80A/Y82A/M207G triple mutant is 4fold larger than that of the wild-type pentaketide chromone synthase. The mutant not only catalyzes the iterative condensation of nine molecules of malonyl-CoA, to produce anovel nonaketide naphthopyrone, but also alters the mechanism of the cyclization to produce the angular naphthopyrone with a fused tricyclic ring system
M197G
-
site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing SEK4/SEK4b like oktaketide synthase
M207G
M207G/N218A
-
site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G
M207G/N218D
-
site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G
M207G/N218E
-
site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G
M207G/N218K
-
site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G
M207G/N218Q
-
site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G
additional information
-
oktaketide synthase, EC 2.3.1.-, and pentaketide chromone synthase, EC 2.3.1.216, are not functionally interconvertible by the single amino acid switch at residue 207