CLONING AND SEQUENCING OF THE GENE FOR A LACTOCOCCAL ENDOPEPTIDASE, AN ENZYME WITH SEQUENCE SIMILARITY TO MAMMALIAN ENKEPHALINASE

Igor Mierau, Paris S.T. Tan, Alfred J. Haandrikman, Jan Kok, Kees J. Leenhouts, Wil N. Konings, Gerard Venema

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Abstract

The gene specifying an endopeptidase of Lactococcus lactis, named pepO, was cloned from a genomic library of L. lactis subsp. cremoris P8-247 in lambdaEMBL3 and was subsequently sequenced. pepO is probably the last gene of an operon encoding the binding-protein-dependent oligopeptide transport system Of L. lactis. The inferred amino acid sequence of PepO showed that the lactococcal endopeptidase has a marked similarity to the mammalian neutral endopeptidase EC 3.4.24.11 (enkephalinase), whereas no obvious sequence similarity with any bacterial enzyme was found. By means of gene disruption, a pepO-negative mutant was constructed. Growth and acid production of the mutant strain in milk were not affected, indicating that the endopeptidase is not essential for growth of L. lactis in milk.

Original languageEnglish
Pages (from-to)2087-2096
Number of pages10
JournalJournal of Bacteriology
Volume175
Issue number7
Publication statusPublished - Apr-1993

Keywords

  • LACTIS SUBSP LACTIS
  • BOVINE BETA-CASEIN
  • CELL-WALL PROTEINASES
  • AMINO-ACID SEQUENCE
  • DIPEPTIDYL AMINOPEPTIDASE GENE
  • DAIRY STARTER CULTURES
  • NEUTRAL ENDOPEPTIDASE
  • STREPTOCOCCUS-CREMORIS
  • MOLECULAR-CLONING
  • SALMONELLA-TYPHIMURIUM

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