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Results 1 - 10 of 18 > >>
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EC Number Protein Variants Commentary Reference
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212C197G site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme 721796
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212C197T site-directed mutagenesis, the mutant shows an unaltered product pattern compared to the wild-type enzyme 721796
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212G256L site-directed mutagenesis, the mutant shows 50% reduced activity but an unaltered product pattern compared to the wild-type enzyme 721796
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212I214L/L215F site-directed mutagenesis, the mutant restores chalcone-forming activity 721796
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212I214L/L215F site-directed mutagenesis, the mutation restores the active site residues of chalcone synthase, the mutant shows chalcone-forming activity, EC 2.3.1.74. The mutant enzyme thus exhibits 36fold decreases in kcat/Km for 4-coumaroyl-CoA and 20fold decreases in kcat/Km for malonyl-CoA compared with wild-type BAS, kinetics of chalcone naringenin-forming activity at pH 6.5, overview 722633
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212L132A site-directed mutagenesis, the substitution expands the product chain length to produce 4-coumaroyltriacetic acid lactone after three condensations with malonyl-CoA, but without the formation of the aromatic ring system 721798
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212L132C site-directed mutagenesis, the substitution expands the product chain length to produce 4-coumaroyltriacetic acid lactone after three condensations with malonyl-CoA, but without the formation of the aromatic ring system 721798
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212L132F site-directed mutagenesis, replacement of Leu132 with bulky aromatic residues, Phe, Tyr and Trp, causes a 1.2fold increase in the benzalacetone-forming activity at pH 8.0, whereas the bisnoryangonin-forming activity is retained or significantly decreased at pH 6.5 721798
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212L132G site-directed mutagenesis, no altered activity compared to the wild-type enzyme 721798
Show all pathways known for 2.3.1.212Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.212L132P site-directed mutagenesis, the L132P mutant exhibits drastically decreased benzalacetone- and bisnoryangonin-forming activities 721798
Results 1 - 10 of 18 > >>
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