Molecular characterization of an Escherichia coli mutant with a temperature‐sensitive malonyl coenzyme A‐acyl carrier protein transacylase

FEBS Letters

van der Linden, Karin H.¹  Stuitje, Antoine R.¹  Verwoert, Ira I.G.S.¹  Nijkamp, H.John J.¹  Verbree, Elizabeth C.¹  Verhagen, Etienne F.¹ 

[1] Department of Genetics, Institute for Molecular Biological Sciences, BioCentrum Amsterdam, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands

关键词: Escherichia coli;    Fatty acid biosynthesis;    Temperature-sensitive;    Malonyl CoA-ACP transacylase;   

DOI  :  10.1016/0014-5793(94)00630-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown