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Cited by 75Enzyme Production and CharacterizationProbiotics and Fermented FoodsBacterial Genetics and Biotechnology

Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp. cremoris are related to secondary binding specificity.

Exterkate, FredA.·1990·Applied Microbiology and Biotechnology
DOI 10.1007/bf00176654
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Abstract

Various chromophoric peptides have been tested as substates for two genetically related types (PI and PIII) of cell-envelope proteinases of Lactococcus lactis subsp. cremoris. The positively charged peptide methoxy-succinyl-arginyl-prolyl-tyrosyl-p-nitroanilide appeared to be cleaved with the highest catalytic efficiency by both enzymes, although in the case of PIII only at high ionic strength. A cation binding site in the PI-type proteinase that is not present in the related PIII-type appears to be mainly responsible for the difference between these enzymes with respect to the rate of conversion of this chromophoric substrate at relatively low ionic strength. This cation binding site most probably resides in the aspartic acid residue 166, which in PIII is substituted by asparagine. Substitution of the threonine residue 138 by lysine in PIII may also play a role. The binding step in the reaction pathway catalysed by PI at low ionic strength is governed mainly by an ionic interaction involving the cation binding site. In addition, hydrophobic interactions contribute to the binding process. Masking of the cation binding site only increases the Michaelis constant Km; the catalytic constant kcat is not affected. In the absence of the cation binding site (viz. in PIII) the free energy derived from the hydrophobic interactions only is too small to promote binding of the substrate effectively. High activities are measured only if a high ionic strength is introduced. Removal of electrostatic repulsion between the substrate and positively charged residues of the enzyme, among which is lysine 138, may contribute to this activation.(ABSTRACT TRUNCATED AT 250 WORDS)

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  • The CEP enzymes are very selective regarding short peptide substrates; most chromogenic substrates are not cleaved at all, and the few cleaved require particular salt concentrations and have specific activity orders of magnitude lower than subtilisin.

    “The CEP enzymes are very selective regarding short peptide substrates. Most chromogenic substrates are not cleaved at all; and the few substrates which are cleaved, require particular salt concentrations; and the specific activity is orders of magnitude lower than for subtilisin (Exterkate, 1990)”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Exterkate, 1990

  • The CEP enzymes cleave only at very few positions within the peptide αS1(1-23).

    “The CEP enzymes cleave only at very few positions within the peptide αS1(1–23) (Exterkate, 1990)”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Exterkate, 1990

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Authors
Exterkate, F.
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
1990-07
Volume
33
Issue
4
Pages
401-6
ISSN
  • 0175-7598 (ISSN-L)
  • 1432-0614
DOI
10.1007/bf00176654
OpenAlex
W1966056510
Cited by
75
References
12
Citations by year
2024: 1 · 2020: 1 · 2017: 1 · 2015: 1 · 2014: 1 · 2013: 4 · 2012: 4
FWCI
4.14
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Applied Microbiology and Biotechnology (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 subsp. cremoris, substrate binding specificity, cation binding sites, ionic strength, hydrophobic interactions, electrostatic interactions, catalytic efficiency, substrate binding
MeSH terms
Butanols, Binding Sites, Calcium, Cell Membrane, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Serine Endopeptidases, Streptococcus, Substrate Specificity, 1-Butanol

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