The gene coding for the proline iminopeptidase (Pip) of pv. was cloned in an strain using a selective medium containing the dipeptide D-Ala-L-Leu as the sole source of L-leucine. Nucleotide sequencing of this gene revealed a 939 bp open reading frame encoding a 312 amino acid protein (35 126 Da). The deduced amino acid sequence showed 47% identity with the Pip from A fusion gene was overexpressed in under the control of the promoter. The Pip of hydrolysed L-prolyl--nitroanilide with the highest efficiency, but was also able to hydrolyse L-alanyl--nitroanilide and D-alanyl--nitroanilide. The molecular mass of Pip was found to be 35 kDa by SDS-PAGE and 120 kDa by gel filtration, suggesting that the active enzyme is a multimer.


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