Abstract
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.
MeSH terms
-
Acyltransferases / genetics*
-
Acyltransferases / metabolism*
-
Amino Acid Sequence
-
Binding Sites
-
Brassica / enzymology
-
Brassica / genetics*
-
Escherichia coli / enzymology
-
Escherichia coli / growth & development
-
Isoenzymes / genetics
-
Isoenzymes / metabolism
-
Microsomes / enzymology
-
Mutagenesis
-
Mutagenesis, Site-Directed
-
Plastids / enzymology*
-
Recombinant Proteins / metabolism
-
Sequence Deletion
-
Templates, Genetic
Substances
-
Isoenzymes
-
Recombinant Proteins
-
Acyltransferases
-
2-acylglycerophosphate acyltransferase