EC Number |
Protein Variants |
Reference |
---|
2.3.1.216 | 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 |
722034 |
2.3.1.216 | M197G |
site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing SEK4/SEK4b like oktaketide synthase |
722089 |
2.3.1.216 | M207G |
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 |
721180 |
2.3.1.216 | M207G |
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 |
722017 |
2.3.1.216 | M207G |
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 |
722034 |
2.3.1.216 | 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 |
722017 |
2.3.1.216 | 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 |
722017 |
2.3.1.216 | 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 |
722017 |
2.3.1.216 | 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 |
722017 |
2.3.1.216 | 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 |
722017 |