Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor.

摘要: The leucine aminopeptidase of Aeromonas proteolytica (EC 3.4.11.10) is a monomeric metalloenzyme having the capacity to bind two Zn2+ atoms in active site. Structural information this relatively small that could illuminate catalytic mechanism metal ions lacking; hence, we have obtained sequences from purified enzyme, cloned corresponding gene, and expressed recombinant protein Escherichia coli. deduced primary amino acid sequence secreted protease suggests potential signal peptide at NH2 terminus. Expression native proteins E. coli extracts culture media A. indicates as an thermosensitive 43-kDa rapidly transformed thermostable forms 30 32 kDa. Comparison with other Zn(2+)-binding metalloenzymes failed show homologies consensus binding His-Glu-X-X-His for ion.