A note on the identity of porcine liver carboxylesterase and prolyl-beta-naphthylamidase

Biol Chem Hoppe Seyler. 1993 Nov;374(11):1033-6. doi: 10.1515/bchm3.1993.374.7-12.1033.

Abstract

Prolyl-beta-naphthylamidase from porcine liver is compared with the two prevalent isoenzymes of pig liver carboxylesterase by isoelectrofocusing experiments and by inhibition studies with phenyl-methyl-sulfonyl fluoride. The results suggest that prolyl-beta-naphthylamidase is identical with the amide-cleaving isoenzyme of carboxylesterase, not with the usually predominant methyl butyrate-hydrolysing isoenzyme. It is questionable whether the recently published sequence of prolyl-beta-naphthylamidase does belong to this enzyme or to the predominant carboxylesterase without amidase activity. Surprisingly, the amide-cleaving carboxylesterase isoenzymes from rat liver have almost no activity with prolyl-beta-naphthylamide.

Publication types

  • Comparative Study

MeSH terms

  • 2-Naphthylamine / analogs & derivatives
  • 2-Naphthylamine / metabolism
  • Amino Acid Sequence
  • Aminopeptidases / chemistry
  • Aminopeptidases / isolation & purification
  • Aminopeptidases / metabolism*
  • Animals
  • Carboxylesterase
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism*
  • Hydrolysis
  • Isoelectric Point
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Liver / enzymology*
  • Molecular Sequence Data
  • Phenylmethylsulfonyl Fluoride / chemistry
  • Proline / analogs & derivatives
  • Proline / metabolism
  • Rats
  • Swine

Substances

  • Isoenzymes
  • prolyl-beta-naphthylamide
  • Phenylmethylsulfonyl Fluoride
  • Proline
  • 2-Naphthylamine
  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • Aminopeptidases