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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28A138S site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138S mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme 735551
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28A138T site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138T mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme. The A138T substitution has no effect on CAT activity 735551
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28A138V site-directed mutagenesis, the enzyme mutant shows highly increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138V mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme 735551
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28A203G mutant enzyme is less stable than wild-type enzyme 486728
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28A203I mutant enzyme is more thermostable than wild-type 486728
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28C214A 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 31% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme 486737
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28C214D 50% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 85% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme 486737
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28C214E 75% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 84% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme 486737
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28C214F/G219S 95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 81% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme 486737
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.28C214G 80% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 44% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme 486737
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