ArticleFolia microbiologica2009
Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp. paracasei.
Article in Folia microbiologica, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Characterization of Cell-Envelope Proteinases from TwoBiology · 2022Article
- Angiotensin-I-Converting Enzyme Inhibitory Peptides in Goat Milk Fermented by Lactic Acid Bacteria Isolated from Fermented Food and Breast Milk.Food science of animal resources · 2022Article
- Pneumococcal Extracellular Serine Proteases: Molecular Analysis and Impact on Colonization and Disease.Frontiers in cellular and infection microbiology · 2021Review
- A Systems-Wide Analysis of Proteolytic and Lipolytic Pathways Uncovers The Flavor-Forming Potential of The Gram-Positive BacteriumFrontiers in microbiology · 2020Article
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Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Comparison of cell-wall-bound extracellular proteinases (CEPs) from Lactobacillus paracasei (LBP) ssp. paracasei natural isolates BGHN14, BGAR75 and BGAR76 with Lactococcus lactis (LCL) ssp. cremoris Wg2, in their action on alpha(S1)-, beta- and kappa-casein was done. The CEPs of LBP strains were able to degrade alpha(S1)- and beta-caseins and their caseinolytic specificity depended on the type of buffer used. These CEPs, compared with LCL Wg2, differ in four amino acid residues in small segments predicted to be involved in substrate binding. The most striking features of this comparison are the presence of Ala instead of Ser(329) and the presence of Thr instead of Asn(256) and Ala(299), in the subtilisin-like region of the CEP in LBP natural isolates. Additional conservative amino acid substitution Leu to Ile(364) was found.
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Registered trials
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