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
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2.3.1.216
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polyketide
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arborescens
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aloe
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condensations
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octaketide
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synthases
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nonaketide
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plant-specific
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unnatural
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naphthopyrone
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inert
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chalcone
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medicago
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hexaketide
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sativa
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longest
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iterative
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lining
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molecular biology
- 2.3.1.216
- polyketide
- arborescens
-
aloe
-
condensations
-
octaketide
- synthases
-
nonaketide
-
plant-specific
-
unnatural
-
naphthopyrone
-
inert
- chalcone
-
medicago
-
hexaketide
- sativa
-
longest
-
iterative
-
lining
- molecular biology
Reaction
5 malonyl-CoA = 5 CoA + + 5 CO2 +
Synonyms
PCS, pentaketide chromone synthase
ECTree
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Engineering
Engineering on EC 2.3.1.216 - 5,7-dihydroxy-2-methylchromone synthase
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F80A/Y82A/M207G
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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
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site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing SEK4/SEK4b like oktaketide synthase
M207G
M207G/N218A
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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
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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
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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
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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
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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
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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
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site-directed mutagenesis, the mutant enzyme efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one, i.e. SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution
M207G
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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 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one, i.e. 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
M207G
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site-directed mutagenesis, the pentaketide chromone synthase M207G mutant no longer produces the pentaketide chromone but instead efficiently catalyzes sequential condensations of eight molecules of malonyl-CoA to produce a 1:4 mixture of the octaketides SEK4/SEK4b. The pentaketide-producing pentaketide chromone synthaseis thus transformed into an octaketide synthase by the single-amino acid replacement