Mechanism and energetics of dipeptide transport in membrane vesicles of Lactococcus lactis
Open accessAbstract
Alanyl-alpha-glutamate transport has been studied in Lactococcus lactis ML3 cells and in membrane vesicles fused with liposomes containing beefheart cytochrome c oxidase as a proton-motive-force-generating system. The uptake of Ala-Glu observed in de-energized cells can be stimulated 26-fold upon addition of lactose. No intracellular dipeptide pool could be detected in intact cells. In fused membranes, a 40-fold accumulation of Ala-Glu was observed in response to a proton motive force. Addition of ionophores and uncouplers resulted in a rapid efflux of the accumulated dipeptide, indicating that Ala-Glu accumulation is directly coupled to the proton motive force as a driving force. Ala-Glu uptake is an electrogenic process and the dipeptide is transported in symport with two protons. In both fused membranes and intact cells the same affinity constant (0.70 mM) for Ala-Glu uptake was found. Accumulated Ala-Glu is exchangeable with externally added alanyl-glutamate, glutamyl-glutamate, and leucyl-leucine, while no exchange occurred upon addition of the amino acid glutamate or alanine. These results indicate that the Ala-Glu transport system has a broad substrate specificity.
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Only very few of the previously reported peptides are small enough to be taken up by the peptide transport systems of L. lactis.
“Only very few of these reported peptides are small enough to be taken up by the peptide transport systems of L. lactis (17, 38, 45).”
From The extracellular PI-type proteinase of Lactococcus lactis hydrolyzes beta-casein into more than one hundred different oligopeptides (1995) · cites this paper as [38]
The available Abstract reports uptake of a dipeptide by L. lactis, but it does not give a peptide-size cutoff or assess how many of the previously reported peptides could be transported. Searches for a size limit and for the claim’s wording found no relevant passage; the available copy shows an abstract and references, not the article body. (LLM, conf=0.72)
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Cloning, expression, and characterization of lactic acid bacteria recombinant prolidases
Yang, S. I. (2007) · University Library - University of Saskatchewan (University of Saskatchewan)
- Authors
- Smid, E. J., Driessen, A. J., & Konings, W. N.
- Affiliations
- University of Groningen (NL)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1989-01
- Volume
- 171
- Issue
- 1
- Pages
- 292-298
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC209585
- OpenAlex
- W1831628839
- Cited by
- 78
- References
- 31
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2021: 1 · 2016: 1 · 2015: 1 · 2014: 1 · 2012: 4
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- Funders
- Rijksuniversiteit Groningen
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- dipeptide transport, Lactococcus lactis, proton motive force, membrane vesicles, cytochrome c oxidase, proton symport, electrogenic transport, substrate specificity, amino acid uptake
- MeSH terms
- Amino Acids, Biological Transport, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Cell Membrane, Dipeptides, Glutamates, Kinetics, Liposomes, Membrane Potentials, Nigericin, Lactococcus lactis, Valinomycin
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