PMID:15820980
| Citation |
Lassila, JK, Keeffe, JR, Oelschlaeger, P and Mayo, SL (2005) Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity. Protein Eng. Des. Sel. 18:161-3 |
|---|---|
| Abstract |
Computational protein design methods were used to predict five variants of monofunctional Escherichia coli chorismate mutase expected to maintain catalytic activity. The variants were tested experimentally and three active site mutants exhibited catalytic activity similar to or greater than the wild-type enzyme. One mutant, Ala32Ser, showed increased catalytic efficiency. |
| Links |
PubMed Online version:10.1093/protein/gzi015 |
| Keywords |
Alanine/genetics; Amino Acid Substitution/genetics; Catalysis; Catalytic Domain; Chorismate Mutase/genetics; Chorismate Mutase/metabolism; Computational Biology; Escherichia coli/enzymology; Mutation; Protein Engineering; Serine/genetics |
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