Crystallization (Comment) | Organism |
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crystal structure analysis, molecular replacement | Aloe arborescens |
Protein Variants | Comment | Organism |
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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 | Aloe arborescens |
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 | Aloe arborescens |
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 | Aloe arborescens |
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 | Aloe arborescens |
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 | Aloe arborescens |
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 | Aloe arborescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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5 malonyl-CoA | Aloe arborescens | - |
5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
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Aloe arborescens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5 malonyl-CoA | - |
Aloe arborescens | 5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | crystal structure analysis, molecular replacement, structure comparison, overview | Aloe arborescens |
Synonyms | Comment | Organism |
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PCS | - |
Aloe arborescens |
pentaketide chromone synthase | - |
Aloe arborescens |
General Information | Comment | Organism |
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evolution | pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases | Aloe arborescens |
additional information | pentaketide chromone synthase residue Met207 is fairly flexible and adopts at least two distinct conformations, active site structure, catalytic residues of pentaketide chromone synthase are V351, M207, and L266, overview. Residues Cys143, Thr204, Met207, Leu266, and Val351 influence the catalytic activity and differentiate the enzyme from chalcone synthase, EC 2.3.1.74. The pentaketide chromone synthase crystal structure reveals neither a hydrogen-bond network, nor any additional catalytic Cys residues that appears to be crucial for the enzyme reaction | Aloe arborescens |