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Results 1 - 10 of 17 > >>
EC Number Protein Variants Commentary Reference
Display the reaction diagram Show all sequences 4.99.1.9E264Q 21% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9E264V less than 1% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9H183A less than 1% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9H183C less than 1% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9H88A 5% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9K87A 92% of wild-type activity 678312
Display the reaction diagram Show all sequences 4.99.1.9more all the non-wild-type LmCpfC variants prove to have a significantly higher koff and consequently a lower affinity. This weaker binding is also reflected in the kon-rate, which is the highest for both tested porphyrin ligands for the wild-type protein 771075
Display the reaction diagram Show all sequences 4.99.1.9R29L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme 771075
Display the reaction diagram Show all sequences 4.99.1.9R45L site-directed mutagenesis, the mutant lacks the H-bonding with the propionate at position 6 (p6), determination and analysis of the mutant enzyme structure as apo-enzyme and with bound substrate coproporphyrin III, structure comparison with the wild-type enzyme, overview 775669
Display the reaction diagram Show all sequences 4.99.1.9R45L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme 771075
Results 1 - 10 of 17 > >>