The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase

FEBS Lett. 1991 Nov 18;293(1-2):37-41. doi: 10.1016/0014-5793(91)81147-z.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases / chemistry
  • Aminopeptidases / genetics*
  • Aminopeptidases / isolation & purification
  • Animals
  • Base Sequence
  • Carboxylesterase
  • Carboxylic Ester Hydrolases / genetics*
  • DNA / isolation & purification
  • Microsomes, Liver / enzymology*
  • Molecular Sequence Data
  • Rabbits
  • Rats
  • Sequence Homology, Nucleic Acid*
  • Substrate Specificity
  • Swine

Substances

  • DNA
  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • Aminopeptidases

Associated data

  • GENBANK/S62644
  • GENBANK/S62648
  • GENBANK/S62652
  • GENBANK/S66780
  • GENBANK/X58803
  • GENBANK/X63322
  • GENBANK/X63323
  • GENBANK/X63567
  • GENBANK/X63568
  • GENBANK/X63569