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Cloning and sequencing of pepC, a cysteine aminopeptidase gene from Lactococcus lactis subsp. cremoris AM2.
Station de Recherches Laitières, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
A gene coding for an aminopeptidase (PepC) from Lactococcus lactis subsp. cremoris AM2 was cloned by complementation of an Escherichia coli mutant lacking aminopeptidase activity. The nucleotide sequence was determined. A portion of the predicted amino acid sequence of PepC (436 amino acids) showed strong homology to the active site of cysteine proteases. No signal sequence was found, indicating an intracellular location of the enzyme.
PMID: 8439160 [PubMed - indexed for MEDLINE]
PMCID: PMC202100
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Cited by 10 PubMed Central articles
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Transcriptional pattern of genes coding for the proteolytic system of Lactococcus lactis and evidence for coordinated regulation of key enzymes by peptide supply.
Guédon E, Renault P, Ehrlich SD, Delorme C.
J Bacteriol. 2001 Jun; 183(12):3614-22.
[J Bacteriol. 2001]
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Atypical genetic locus associated with constitutive production of enterocin B by Enterococcus faecium BFE 900.
Franz CM, Worobo RW, Quadri LE, Schillinger U, Holzapfel WH, Vederas JC, Stiles ME.
Appl Environ Microbiol. 1999 May; 65(5):2170-8.
[Appl Environ Microbiol. 1999]
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Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity of the thiol aminopeptidase PepC, a bacterial bleomycin hydrolase.
Mata L, Erra-Pujada M, Gripon JC, Mistou MY.
Biochem J. 1997 Dec 1; 328 ( Pt 2):343-7.
[Biochem J. 1997]
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