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Home >>Protein Engineering, Immunotoxins and Drug Designing - Engineering of Macromolecules >> Mutagenesis and Selection for Protein Engineering
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Mutagenesis and Selection for Protein Engineering - Mutagenesis and selection can be effectively utilized for improving a specific property of an enzyme. Following are some of the examples of selection of mutant enzymes:

(i) E. coli anthranilate synthetase enzyme is normally sensitive to tryptophan inhibition due to feedback inhibition. An MTR 2 mutation of E. coli was found to possess an altered form of enzyme anthranilate synthetase that is insensitive to tryptophan inhibition. They may help in continuous synthesis of tryptophan without any inhibition by tryptophan accumulated as a product.

(ii) Xanthine dehydrogenase enzyme oxidizes 2 hydroxy-purine at position 8, but a mutant has been inolated which oxidizes 2 hydroxy-purine at position 6.

(iii) Lactate dehydrogenase (LDU) from a bacterial system was modified to malate dehydrogenase able a natural mutation leading to a single amino acid substitution (Gln 02... Arg; see later m thIS chapter).

In the above and other cases of naturally occurring mutant enzymes, single amino acid modification or addition/deletion has been observed.

However, if improvement requires changes in several amino acids, such a mutant will be rare or nonexistent and modifications of this type will be possible only through gene modification techniques discussed in the following section.