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Results 1 - 10 of 11 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216F80A/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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M197G site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing SEK4/SEK4b like oktaketide synthase 722089
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G 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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G 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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G 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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G/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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G/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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G/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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G/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
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.216M207G/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
Results 1 - 10 of 11 > >>