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Results 1 - 7 of 7
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67D243A site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme 669041
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67E177D site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme 669041
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67M98I site-directed mutagenesis, the kinetics of the mutant enzyme are similar to those of the wild-type enzyme 669041
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67more construction of chimera between chrysanthemyl diphosphate synthase CPPase and farnesyl diphosphate synthase FPPase, EC 2.5.1.10 by sequentially replacing the loops and helices of the six-helix bundle from one enzyme with those from the other. Chain elongation is the dominant activity during the N-terminal to C-terminal metamorphosis of FPPase to CPPase, with product selectivity gradually switching from FPP to GPP, until replacement of the final alpha-helix, where upon cyclopropanation and branching activity compete with chain elongation. During the metamorphosis of CPPase to FPPase, cyclopropanation and branching activities are lost upon replacement of the first helix in the six-helix bundle. Mutations of active site residues in CPPase to the corresponding amino acids in FPPase enhance chain-elongation activity, while similar mutations in the active site of FPPase fail to significantly promote formation of significant amounts of irregular monoterpenes 759401
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67more construction of mutant enzymes as CPPase-FPPase chimeras with the larger domains of CPPase substituted for FPPase in the Artemisia tridentata enzyme, the CPPase-FPPase chimeras are biosynthetically more promiscuous than either native CPPase or FPPase as a result of a reshaped template for substrate binding, which permits alternative trajectories for intermolecular carbon-carbon bond formation, overview 670890
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67N283D site-directed mutagenesis, replacing the asparagine with either aspartate or glycine in the aspartate-rich motif abolishes the enzyme's terpene synthase and prenyltransferase activities 738635
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.67N283G site-directed mutagenesis, replacing the asparagine with either aspartate or glycine in the aspartate-rich motif abolishes the enzyme's terpene synthase and prenyltransferase activities 738635
Results 1 - 7 of 7