Biochemical and molecular characterization of PepR, a dipeptidase, from Lactobacillus helveticus CNRZ32
نویسندگان
چکیده
منابع مشابه
Characterization of a thiol-dependent endopeptidase from Lactobacillus helveticus CNRZ32.
An endopeptidase gene (pepE) was isolated from a previously constructed genomic library of Lactobacillus helveticus CNRZ32. The pepE gene consisted of a 1,314-bp open reading frame encoding a putative peptide of 52.1 kDa. Significant identity was found between the deduced amino acid sequence of pepE and the sequences for aminopeptidase C from Lactobacillus delbrueckii subsp. lactis DSM7290, L. ...
متن کاملGenetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32.
A cell envelope-associated proteinase gene (prtH) was identified in Lactobacillus helveticus CNRZ32. The prtH gene encodes a protein of 1,849 amino acids and with a predicted molecular mass of 204 kDa. The deduced amino acid sequence of the prtH product has significant identity (45%) to that of the lactococcal PrtP proteinases. Southern blot analysis indicates that prtH is not broadly distribut...
متن کاملGenetic characterization and physiological role of endopeptidase O from Lactobacillus helveticus CNRZ32.
A previously identified insert expressing an endopeptidase from a Lactobacillus helveticus CNRZ32 genomic library was characterized. Nucleotide sequence analysis revealed an open reading frame of 1,941 bp encoding a putative protein of 71.2 kDa which contained a zinc-protease motif. Protein homology searches revealed that this enzyme has 40% similarity with endopeptidase O (PepO) from Lactococc...
متن کاملMolecular characterization of a stress-inducible gene from Lactobacillus helveticus.
A gene (htrA) coding for a stress-inducible HtrA-like protein from Lactobacillus helveticus CNRZ32 was cloned, sequenced, and characterized. The deduced amino acid sequence of the gene exhibited 30% identity with the HtrA protein from Escherichia coli; the putative catalytic triad and a PDZ domain that characterize the HtrA family of known bacterial serine proteases were also found in the seque...
متن کاملNucleotide sequence and distribution of the pepPN gene from Lactobacillus helveticus CNRZ32.
The Lactobacillus helveticus CNRZ32 gene encoding a di-/tri- pepidase with prolinase activity (pepPN) was sequenced. An open reading frame of 912 base pairs was identified corresponding to a peptide with a molecular mass of 35.04 kDa. Southern hybridization indicated that the gene sequence is well conserved in strains of lactobacilli and pediococci.
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1997
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.63.9.3438-3443.1997