Amplification, cloning and sequencing of Enterococcus feacalis enolase gene

Abstract

307-312α-Enolase, a key glycolytic enzyme, belongs to a novel class of surface proteins, which do not possess classical machinery for surface transport and transported on the cell surface through an unknown mechanism. It is a multifunctional protein and its ability to serve as a plasminogen receptor on the surface of a variety of hematopoetic, epithelial and endothelial cells suggest that it may play an important role in the intravascular and pericellular fibrinolytic system. Authors have amplified and cloned α-enolase gene of Enterococcus feacalis in a prokaryotic cloning vector, and then transferred it into Escherichia coli. The recombinant enolase vector (r-pBEnol) was isolated and sequenced. The sequence of the cloned enolase from E. feacalis was found identical to that of the E. feacalis V583. The sequence was submitted to NCBI nucleotide data bank and accession number (AM279410) was obtained