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Results 1 - 10 of 10
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9K478A catalytic activity 1/200 of the wild-type enzyme -, 698757
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9M142A kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased -, 698757
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9R143A inactive -, 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9R143A mutant enzyme shows no activity -, 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9R143K mutant enzyme shows 400fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants -, 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9R143K the mutant has about 400fold lower activity than the wild type enzyme -, 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9Y536A inactive 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9Y536A mutant enzyme shows no activity 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9Y536F mutant enzyme shows 17fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants -, 727793
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.9Y536F the mutant has about 17fold lower activity than the wild type enzyme 727793
Results 1 - 10 of 10