f Cloning, sequencing and characterization of the pepIP gene encoding a proline iminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397
- Authors: Danièle Atlan5, Christophe Gilbert, Brigitte Blanc, Raymond Portalier
- 5Author for correspondence: Danièle Atlan. Tel: +33 72 44 81 05. Fax: +33 72 43 11 81. e-mail: firstname.lastname@example.org-Lyon1.fr
- First Published Online: 01 March 1994, Microbiology 140: 527-535, doi: 10.1099/00221287-140-3-527
- Subject: Genetics And Molecular Biology
- Issue Published:
The proline iminopeptidase (PepIP) of Lactobacillus delbrueckii subsp. bulgaricus is a major peptidase located in the cell envelope. Its structural gene (pepIP) has been cloned into pUC18 and expressed at a very high level in Escherichia coli to give a PepIP activity 15000-fold higher than that found in L. delbrueckii subsp. bulgaricus. The nucleotide sequence of the pepIP gene revealed an open reading frame of 295 codons encoding a protein with a predicted M r of 33006, which is consistent with the apparent size of the gene product. The amino acid sequence of PepIP shows significant homology with those of other hydrolases involved in the degradation of cyclic compounds. In particular, there is a region which includes an identified catalytic site containing a serine residue and a motif specific for the active sites of prolyloligopeptidases (Gly-X-Ser-X-Gly-Gly). The PepIP opens a new way for supplying cells with proline using the peptides resulting from the proteolytic degradation of caseins.
- Keyword(s): casein hydrolysis, proline iminopeptidase, Lactobacillus delbrueckii subsp. bulgaricus, prolyl oligopeptidases
© Society for General Microbiology 1994 | Published by the Microbiology Society
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/content/journal/micro/10.1099/00221287-140-3-527dcterms_title,dcterms_subject-pub_serialIdent:journal/micro AND -contentType:BlogPost104
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