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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274E236A site-directed mutagenesis 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274K184A site-directed mutagenesis 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274K184Q site-directed mutagenesis 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274K184R site-directed mutagenesis -, 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274K233A site-directed mutagenesis -, 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274N229A site-directed mutagenesis, the mutation causes the greatest kcat decrease by more than 10fold and increases KM by 4.4 and 2.6fold for palmitoyl-ACP and phosphate, respectively -, 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274N229Q site-directed mutagenesis, most of the catalytic activity of mutant N229A is recovered with a 2.2fold KM increase for palmitoyl-ACP when glutamine is introduced into the mutated position in N229Q 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274R114A site-directed mutagenesis, the catalytic activity of the negative control mutant protein R114A is essentially the same compared to wild-type enzyme for both substrates -, 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274R120A site-directed mutagenesis, the mutation causes a significant 3.3fold increase in KM for palmitoyl-ACP without adverse effect on other kinetic constants 756464
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.274R73A site-directed mutagenesis, the mutation causes a significant 2.5fold increase in KM for palmitoyl-ACP without adverse effect on other kinetic constants -, 756464
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