Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: sequence analysis and over-expression in Escherichia coli.
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 lambda. 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. lwoffii RAG-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.
Alon
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Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Israel.
Gutnick
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D000150:Acinetobacter / Q000235:genetics*; D000595:Amino Acid Sequence; D001673:Biodegradation, Environmental; D002451:Cell Compartmentation; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D004950:Esterases / Q000096:biosynthesis / Q000235:genetics*; D005798:Genes, Bacterial; D008049:Lipase / Q000235:genetics; D008969:Molecular Sequence Data; D010578:Petroleum; D011994:Recombinant Proteins / Q000096:biosynthesis; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics
D010578:Petroleum; D011994:Recombinant Proteins; D004950:Esterases; C084091:RAG-1 esterase; D008049:Lipase; D012697:Serine Endopeptidases