The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.
Open accessAbstract
The biochemical and genetical diversity of the subtilisin-like cell envelope proteinase (CEP) among Lactococcus lactis strains was investigated. The specificities of the proteinases of 16 strains toward the important cheese peptide alpha s1-casein fragment 1 to 23 and toward two differently charged chromophoric peptides have been determined. On the basis of the results, these strains could be classified into seven groups. The contribution to the specificity of specific residues in the large C-terminal segment, which differentiates this proteinase from most other members of the subtilisin family, was established with hybrid proteinases, even in the case of the small substrates. These remote residues and the subtilisin-like substrate-binding region are therefore assumed to be spatially close to each other and together constitute most of the binding region of CEP. DNA sequence analysis of fragments of the gene (prtP) encoding segments of the proteinase which contain the relevant residues of the substrate-binding region shows that among the strains studied, this binding region is the most negatively charged in the CEP group represented by strain HP and the positively charged in the CEP group represented by strains AM1 and SK11. Consequently, these two proteinase groups show the most divergent specificities. Each of the proteinases of the other groups shows a different intermediate specificity which in part is the reflection of an intermediate charge in the binding region. However, the results suggest that amino acid residues outside the segments known to be part of the CEP-binding region also contribute to specificity.(ABSTRACT TRUNCATED AT 250 WORDS)
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“Some PrtP enzymes (PI type) prefer β-casein and all types cleave β- casein at multiple sites with no obvious specificity (Visser et al., 1986; Exterkate et al., 1993; Børsting et al., 2015).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Exterkate et al., 1993
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PRINCIPLES THAT DETERMINE THE STRUCTURE OF PROTEINS
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Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391
Biochemistry of cheese ripening
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Kunji, E. R. S., Mierau, I., Hagting, A., Poolman, B., & Konings, W. N. (1996) · Antonie van Leeuwenhoek · doi:10.1007/bf00395933 · Cited by 724
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Proteolysis in Cheese during Ripening
Upadhyay, V. K., McSweeney, P. L. H., Magboul, A. A. A., & Fox, P. F. (2004) · Cheese · doi:10.1016/s1874-558x(04)80076-9 · Cited by 208
Metadata
- Authors
- Exterkate, F. A., Alting, A. C., & Bruinenberg, P. G.
- Affiliations
- Nederlands Instituut Voor Zuivel Oonderzoek (NL)
- Department of Biophysical Chemistry, Netherlands Institute for Dairy Research (NIZO), Ede.
- ORCID
- Alting, A C
- Venue
- Applied and Environmental Microbiology
- Publisher
- American Society for Microbiology
- Published
- 1993-11
- Volume
- 59
- Issue
- 11
- Pages
- 3640-3647
- ISSN
- 0099-2240 (ISSN-L)
- 1098-5336
- PMC
- PMC182510
- OpenAlex
- W1558188999
- Cited by
- 126
- References
- 29
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 1 · 2023: 5 · 2022: 1 · 2021: 2 · 2020: 6 · 2019: 1 · 2018: 1 · 2017: 7 · 2016: 1 · 2014: 6 · 2012: 7
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Applied and Environmental Microbiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Lactococcus lactis, cell envelope proteinase, protease specificity, substrate-binding region, charge characteristics, αs1-casein, cheese peptides, strain classification
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Caseins, DNA, Bacterial, Electrochemistry, Molecular Sequence Data, Peptide Fragments, Serine Endopeptidases, Species Specificity, Lactococcus lactis, Substrate Specificity, Genetic Variation, DNA Primers
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