expression cloning strategy to isolate the sialidase. The clone encodes a 990-amino-acid 104 kDa open-reading-frame protein containing three domains: an N-terminal catalytic domain, a linker domain with an immunoglobulin-like fold and a C-terminal domain of unknown function. Expression in Escherichia coli indicates that the sialidase promoter is active in Escherichia coli. Overexpression in Escherichia coli resulted in several truncated forms. 54 kDa truncated variant is generated, expressed and purified |
Paenarthrobacter ureafaciens |