Abstract
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.
Original language | English |
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Pages (from-to) | 275-280 |
Number of pages | 6 |
Journal | FEMS Microbiology Letters |
Volume | 112 |
Issue number | 3 |
DOIs | |
State | Published - 15 Sep 1993 |
Keywords
- Acinetobacter lwoffi
- Escherichia coli
- Esterase
- Lipase
- Overexpression
- Serine protease