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The molecular mass of the bacterial oligopeptidase activity (77-78 kDa) was decided by gel filtration, and the impact of inhibitors, together with captopril, urged that it results from a combination of oligopeptidase A (OpdA) and peptidyl dipeptidase Dcp (77.1 and 77.5 kDa, respectively). These results suggest that the enzyme is synthesized as an integral membrane protein and is launched into blood beneath some physiological situations. The predicted P-LAP incorporates the HEXXH consensus sequence of zinc metallopeptidases, linked site indicating that the enzyme belongs to this family, which incorporates aminopeptidase N and aminopeptidase A. The deduced sequence additionally comprises a hydrophobic area near the N terminus, suggesting that the enzyme is a kind II integral membrane protein. P-LAP degrades several peptide hormones such as oxytocin and vasopresin, suggesting a role in sustaining homeostasis throughout pregnancy. The amino acid sequence deduced from the cDNA contained the entire sequences of the peptide fragments obtained by digestion of the purified protein with trypsin. Yeast possess an enzyme known as phytase, which reduces phytic acid in grains during fermentation, decreasing the phytic acid content of breads and other fermented foods.

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