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Morand, L.Z. et al.

Morand, Patil, Quasney, German,

Alteration of the fatty acid substrate specificity of lysophosphatidate acyltransferase by site-directed mutagenesis.

The JC201 strain of Eschericia coli contains a temperature-sensitive lesion in lysophosphatidate acyltransferase (LPAT) activity. The LPAT gene from JC201 was isolated by PCR and a single mutant nucleotide, adenine-440, was identified by DNA sequence analysis. Site-directed mutagenesis converted the mutant adenine-440 back to the native guanine-440 nucleotide. The restored LPAT gene rescued JC201 cells at the non-permissive temperature. The fatty acid substrate specificity of LPAT from Eschericia coli was altered by site-directed mutagenesis of a single amino acid in the restored LPAT gene. Threonine-122 of LPAT was changed to alanine or leucine. A change from threonine-122 to alanine increased the substrate specificity in vitro for oleoyl-CoA and linoleoyl-CoA; whereas a change to leucine increased the substrate specificity for lignoceroyl-CoA.[1]

References

Alteration of the fatty acid substrate specificity of lysophosphatidate acyltransferase by site-directed mutagenesis. Morand, L.Z., Patil, S., Quasney, M., German, J.B. Biochem. Biophys. Res. Commun. (1998) [Pubmed]

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