The est gene encoding an esterase from Acinetobacter lwoffii RAG-1 was cloned into E. coli under the control of the PL promoter of the phage λ. The N-terminal sequence of the first 20 amino acids of the heterologous expressed esterase corresponded to that obtained from the nucleotide sequence. Antibodies prepared against the over-expressed recombinant esterase in E.coli were used to locate the enzyme primarily in the membrane fractions of A. lwoffiiRAG-1. Comparison with homologous proteins from both eukaryotic and prokaryotic organisms suggest that the RAG-1 esterase exhibits sequence motifs characteristic of both serine proteases and of lipases.
|Number of pages||6|
|Journal||FEMS Microbiology Letters|
|State||Published - 15 Sep 1993|
- Acinetobacter lwoffi
- Escherichia coli
- Serine protease