CLONING AND NUCLEOTIDE SEQUENCING OF THE AMINOPEPTIDASE GENE FROM AEROMONAS-CAVIAE T-64

The aminopeptidase (apAC) gene from Aeromonas caviae T-64 was cloned a nd sequenced, This gene codes for a polypeptide composed of 393 amino acids with a calculated molecular mass of 42.2 kDa, The deduced polype ptide contains a putative signal sequence followed by a large proprote in which is thought to be processed to the mature 29.7 kDa protein. Th e deduced amino acid sequence showed 56.7% identity with that of the V ibrio proteolyticus aminopeptidase, a metalloenzyme with a capacity fo r binding two Zn2+ per molecule, The C-terminal 'helper domain' consid ered as a requirement for protein excretion, associated with extracell ular proteases From the Vibrionaceae family, was not found in apAC, Ac cordingly, apAC secretion is probably mediated by a different mechanis m.