ArticleApplied and environmental microbiology2003
Identification and characterization of Lactobacillus helveticus PepO2, an endopeptidase with post-proline specificity.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 40 citations in OpenAlex.
- The Enzyme Gene Expression of Protein Utilization and Metabolism byMicroorganisms · 2022Article
- Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.Plants (Basel, Switzerland) · 2022Review
- Hydrolytic enzymes and their directly and indirectly effects on gluten and dough properties: An extensive review.Food science & nutrition · 2021Review
- Cross-Talk Between Gluten, Intestinal Microbiota and Intestinal Mucosa in Celiac Disease: Recent Advances and Basis of Autoimmunity.Frontiers in microbiology · 2018Review
- Effect of culturing conditions on the expression of key enzymes in the proteolytic system of Lactobacillus bulgaricus.Journal of Zhejiang University. Science. B · 2015Article
- Dipeptidase activity and growth of heat-treated commercial dairy starter culture.Applied biochemistry and biotechnology · 2015Article
- Lactobacillus helveticus: the proteolytic system.Frontiers in microbiology · 2013Article
- Proteases as therapeutics.The Biochemical journal · 2011Review
- Genome sequence and comparative genome analysis of Lactobacillus casei: insights into their niche-associated evolution.Genome biology and evolution · 2009Article
- Enzymatic ability of Bifidobacterium animalis subsp. lactis to hydrolyze milk proteins: identification and characterization of endopeptidase O.Applied and environmental microbiology · 2005Article
- Identification of endopeptidase genes from the genomic sequence of Lactobacillus helveticus CNRZ32 and the role of these genes in hydrolysis of model bitter peptides.Applied and environmental microbiology · 2005Article
- Hydrolysis of casein-derived peptides alpha(S1)-casein(f1-9) and beta-casein(f193-209) by Lactobacillus helveticus peptidase deletion mutants indicates the presence of a previously undetected endopeptidase.Applied and environmental microbiology · 2003Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A post-proline endopeptidase (PepO2) was detected in cell extracts from a genomic library of Lactobacillus helveticus CNRZ32 by using the synthetic substrate N-acetyl-beta-casein-(f203-209)-rho-nitroanilide in a coupled reaction with aminopeptidase N. Isolates with activity for this substrate contained plasmids with visually indistinguishable restriction profiles. Nucleotide sequence analysis revealed a 1,947-bp open reading frame, designated pepO2, encoding a putative 71.4-kDa protein. Analysis of the predicted peptide sequence revealed that L. helveticus PepO2 contained the zinc-dependent metalloprotease motif HEXXH and exhibited levels of amino acid sequence similarity of 72, 61, 59, and 53% to L. helveticus PepO, Lactococcus lactis PepO2, L. lactis PepO, and Lactobacillus rhamnosus PepO, respectively. Northern hybridization results indicated that the transcript containing pepO2 was monocistronic. Despite the high degrees of amino acid similarity to PepO proteins from other lactic acid bacteria, the specificity of the L. helveticus PepO2 for post-proline bonds distinguishes it from other PepO-type endopeptidases characterized to date. The specificity for post-proline bonds also suggests that this enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209).
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