Cloning and sequencing of the gene for a lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase.

作者: I Mierau , P S Tan , A J Haandrikman , B Mayo , J Kok

DOI: 10.1128/JB.175.7.2087-2096.1993

关键词: BiologyBiochemistryLactococcus lactisOperonNucleic acid sequenceGeneticsPeptide sequenceEndopeptidaseMutantOligopeptide transportGenomic library

摘要: The gene specifying an endopeptidase of Lactococcus lactis, named pepO, was cloned from a genomic library L. lactis subsp. cremoris P8-2-47 in lambda EMBL3 and subsequently sequenced. pepO is probably the last operon encoding binding-protein-dependent oligopeptide transport system lactis. inferred amino acid sequence PepO showed that lactococcal has marked similarity to mammalian neutral EC 3.4.24.11 (enkephalinase), whereas no obvious with any bacterial enzyme found. By means disruption, pepO-negative mutant constructed. Growth production strain milk were not affected, indicating essential for growth milk.

参考文章(0)