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EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195A278V the isoform CAD4 mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme 762157
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195D57A about 4fold increase in catalytic efficiency 726086
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195F226A site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 4fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2 741161
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195G301F the isoform CAD4 mutant enzyme displays slightly elevated Km values for 4-coumaryl aldehyde but decreased Km for coniferyl aldehyde compared with those values of wild type. The mutant becomes more dedicated toward sinapyl aldehyde, with substantially decreased efficiency for coniferyl aldehyde compared to the wild type enzyme 762157
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195G575A/G192D the nucleotide substitution G575A occurs in BdCAD1 of the Bd4179 line, and consequently induces the G192D change in the highly conserved glycine-rich NADPH binding site GLGGVG 741173
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195H52A about 40% decrease in catalytic efficiency 726086
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195K169A site-directed mutagenesis, inactive mutant 741161
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195L119W the isoform CAD4 mutant displays a slightly reduced Km value for both 4-coumaryl aldehyde and coniferyl aldehyde compared to the wild type enzyme. The mutant becomes more efficient toward coniferaldehyde due to the very small Km value, with substantially decreased efficiency for both sinapyl aldehyde and 4-coumaryl aldehyde 762157
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195L119W/G301F the isoform CAD4 double mutant displays its substrate preference in the order coniferyl aldehyde over 4-coumaryl aldehyde over sinapyl aldehyde, with higher catalytic efficiency than that of wild type enzyme. The mutant displays 10 and 800fold increases in its catalytic efficiency for coniferyl aldehyde and 4-coumaryl aldehyde, respectively, and a 50% decrease in catalytic efficiency for sinapyl aldehyde as compared to the wild type enzyme 762157
Show all pathways known for 1.1.1.195Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.195more BdCAD1 targeted silencing via highly specific artificial microRNA, Transgenic growth and developmental phenotype, overview. Downregulation of BdCAD1 is associated with a significant decrease in S units and a slight yet not statistically significant increase in G units, resulting in a reduced S/G ratio in lignin composition 733569
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