Improved heterologous expression of human glutathione transferase A4-4 by random silent mutagenesis of codons in the 5' region.
Glutathione transferase A4-4 (GST A4-4) is involved in the detoxication of lipid peroxidation products such as alkenals. The human enzyme has been heterologously expressed in Escherichia coli, but for more extensive characterization of the enzyme the expression level had to be elevated. A clone providing up to 8-fold higher yields was created, by screening an expression library with random silent mutations in the 5' region of the cDNA encoding GST A4-4.
Nilsson
L O
LO
Department of Biochemistry, Biomedical Center, Uppsala University, Box 576, SE-751 23, Uppsala, Sweden.
Mannervik
B
B
D003062:Codon; D018076:DNA, Complementary / Q000096:biosynthesis; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic; D015723:Gene Library; D005982:Glutathione Transferase / Q000096:biosynthesis* / Q000235:genetics; D006801:Humans; D016296:Mutagenesis; D011994:Recombinant Proteins / Q000096:biosynthesis
D003062:Codon; D018076:DNA, Complementary; D011994:Recombinant Proteins; D005982:Glutathione Transferase; C041116:leukotriene-C4 synthase