Abstract
Human laeverin/aminopeptidase Q (APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of extravillous trophoblasts. In this study, we examined the significance of Gln-238 of laeverin/APQ, a putative S1 site residue, by site-directed mutagenesis for its enzymatic activity and substrate specificity. Replacement of Gln-238 with Ala caused a significant change in substrate specificity rather than a decrease in enzymatic activity. These results indicate that Gln-238 is important for the substrate specificity of laeverin/APQ. In addition, our data suggest that direct electrostatic interaction between substrate and S1 site of the enzyme is not involved in the mutant enzyme's preference for basic amino acids.
