Cited by 126Enzyme Production and CharacterizationProbiotics and Fermented FoodsBacterial Genetics and Biotechnology

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Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.

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Exterkate, F A, Alting, A C, Bruinenberg, P G·1993·Applied and Environmental Microbiology

DOI 10.1128/aem.59.11.3640-3647.1993PMC PMC182510

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Abstract

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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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
DOI: 10.1128/aem.59.11.3640-3647.1993
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.

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