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The general aminopeptidase PepN fromStreptococcus thermophilus A was purified to protein homogeneity by hydroxyapatite, anion-exchange, and gel filtration chromatographies. The PepN enzyme was estimated to be a monomer of 95 kDa, with maximal activity onN -Lys–7-amino-4-methylcoumarin at pH 7 and 37°C. It was strongly inhibited by metal chelating agents, suggesting that it is a metallopeptidase. The activity was greatly restored by the bivalent cations Co2+ , Zn2+ , and Mn2+ . Except for proline, glycine, and acidic amino acid residues, PepN has a broad specificity on theN -terminal amino acid of small peptides, but no significant endopeptidase activity has been detected. TheN -terminal and short internal amino acid sequences of purified PepN were determined. By using synthetic primers and a battery of PCR techniques, thepepN gene was amplified, subcloned, and further sequenced, revealing an open reading frame of 2,541 nucleotides encoding a protein of 847 amino acids with a molecular weight of 96,252. Amino acid sequence analysis of thepepN gene translation product shows high homology with other PepN enzymes from lactic acid bacteria and exhibits the signature sequence of the zinc metallopeptidase family. ThepepN gene was cloned in a T7 promoter-based expression plasmid and the 452-fold overproduced PepN enzyme was purified to homogeneity from the periplasmic extract of the hostEscherichia coli strain. The overproduced enzyme showed the same catalytic characteristics as the wild-type enzyme.

Purification, Characterization, Gene Cloning, Sequencing, and Overexpression of Aminopeptidase N from Streptococcus thermophilus A