A combination of site-directed and random mutagenesis generated sequence variants of a plastidial lysophosphatidic acid acyltransferase. Alanine substitutions of residues present within two conserved motifs including the putative catalytic histidine resulted in a loss of acyltransferase activity assessed as complementation competance. Substitutions at five sites within the central core resulted in reduced or loss of activity. Truncation mutants reveal that sequences in the C-terminal moiety are essential for function.
Mutagenesis of a plastidial lysophosphatidic acid acyltransferase
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S. Maisonneuve, J.-J. Bessoule, R. Lessire, M. Delseny, T. J. Roscoe; Mutagenesis of a plastidial lysophosphatidic acid acyltransferase. Biochem Soc Trans 1 December 2000; 28 (6): 961–964. doi: https://doi.org/10.1042/bst0280961
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