![]() However, the present work shows that the knowledge-based redesign restricted to substrate-binding residues in human glutathione transferase A2-2 can introduce high steroid double-bond isomerase activity into the enzyme originally characterized by glutathione peroxidase activity. Such attempts based on the comparison of similar structures with different substrate selectivities have previously met with limited success. For the engineering of enzymes with novel functions, it would be of great value if the necessary changes of the active site could be predicted and implemented. Successful attempts have frequently been based on directed molecular evolution involving libraries of random mutants in which variants with desired properties were identified. ![]() Pettersson, Par L Johansson, Ann-Sofie Mannervik, BengtĪ major goal in protein engineering is the tailor-making of enzymes for specified chemical reactions. Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.
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