Molecular characterization of an Escherichia coli mutant with a temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase.
The temperature-sensitive malonyl CoA-ACP transacylase found in the Escherichia coli strain LA2-89, carrying the fabD89 allele, was shown to result from the presence of an amber mutation in the fabD gene, at codon position 257, in combination with the supE44 genotype of this strain. The truncated form of the protein produced as the result of the amber mutation was demonstrated to be enzymatically inactive, whereas amber suppression rendered the resulting enzyme temperature labile. Site-directed mutagenesis of codon 257 revealed a requirement for an aromatic amino acid at this position in the polypeptide chain, to assure temperature stability of the enzyme.
Department of Genetics, BioCentrum Amsterdam, Vrije Universiteit, The Netherlands.
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Verwoert
E F
EF
Verhagen
K H
KH
van der Linden
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EC
Verbree
H J
HJ
Nijkamp
A R
AR
Stuitje
D051080:Acyl-Carrier Protein S-Malonyltransferase; D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism; D000483:Alleles; D001483:Base Sequence; D003062:Codon; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins; D054889:Fatty Acid Synthase, Type II; D005227:Fatty Acids / Q000378:metabolism; D006358:Hot Temperature; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D013696:Temperature; D014364:Tryptophan / Q000235:genetics
D003062:Codon; D029968:Escherichia coli Proteins; D005227:Fatty Acids; D014364:Tryptophan; D000217:Acyltransferases; D051080:Acyl-Carrier Protein S-Malonyltransferase; C494968:fabD protein, E coli; D054889:Fatty Acid Synthase, Type II