A cDNA clone for porcine liver proline-beta-naphthylamidase was isolated and sequenced. The deduced amino acid sequence of 567 residues was highly homologous with those of carboxylesterases (EC 3.1.1.1) previously reported for other species. In addition, proline-beta-naphthylamidase purified from porcine liver was shown to have strong activity towards p-nitrophenylacetate, a representative substrate for carboxylesterases. These results suggest that proline-beta-naphthylamidase is identical with carboxylesterase.
Matsushima M, Inoue H, Ichinose M, Tsukada S, Miki K, Kurokawa K, Takahashi T, Takahashi K (1991) The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase FEBS Letters293: 37-41
Matsushima M, Inoue H, Ichinose M, Tsukada S, Miki K, Kurokawa K, Takahashi T, Takahashi K (1991) FEBS Letters293: 37-41