Mutagenesis of a plastidial lysophosphatidic acid acyltransferase.
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 competence. 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.
Maisonneuve
S
S
Laboratoire de Génome et Développement des Plantes, CNRS UMR 5096, Université de Perpignan, 52 Avenue de Villeneuve, 66860 Perpignan, France.
Bessoule
J J
JJ
Lessire
R
R
Delseny
M
M
Roscoe
T J
TJ
D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D001937:Brassica / Q000201:enzymology / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000254:growth & development; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008861:Microsomes / Q000201:enzymology; D016296:Mutagenesis; D016297:Mutagenesis, Site-Directed; D018087:Plastids / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism; D017384:Sequence Deletion; D013698:Templates, Genetic
D007527:Isoenzymes; D011994:Recombinant Proteins; D000217:Acyltransferases; C018764:2-acylglycerophosphate acyltransferase