scholarly journals Kinetics and Specificity of Peptide Uptake by the Oligopeptide Transport System ofLactococcuslactis†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16671-16679 ◽  
Author(s):  
Frank J. M. Detmers ◽  
Edmund R. S. Kunji ◽  
Frank C. Lanfermeijer ◽  
Bert Poolman ◽  
Wil N. Konings
Keyword(s):  
Transport System ◽  
Peptide Uptake ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

Specificity of Milk Peptide Utilization byLactococcus lactis

1998 ◽  
Vol 64 (4) ◽  
pp. 1230-1236 ◽  
Author(s):  
Vincent Juillard ◽  
Alain Guillot ◽  
Dominique Le Bars ◽  
Jean-Claude Gripon
Keyword(s):  
Substrate Specificity ◽  
Transport System ◽  
Time Course ◽  
Solid Phase ◽  
Amino Acid Content ◽  
Defined Medium ◽  
Milk Peptides ◽  
Basic Peptides ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

ABSTRACT To study the substrate specificity of the oligopeptide transport system of Lactococcus lactis for its natural substrates, the growth of L. lactis MG1363 was studied in a chemically defined medium containing milk peptides or a tryptic digest of αs2-casein as the source of amino acids. Peptides were separated into acidic, neutral, and basic pools by solid-phase extraction or by cation-exchange liquid chromatography. Their ability to sustain growth and the time course of their utilization demonstrated the preferential use of hydrophobic basic peptides with molecular masses ranging between 600 and 1,100 Da by L. lactis MG1363 and the inability to use large, acidic peptides. These peptide utilization preferences reflect the substrate specificity of the oligopeptide transport system of the strain, since no significant cell lysis was inferred. Considering the free amino acid content of milk and these findings on peptide utilization, it was demonstrated that the cessation of growth of L. lactis MG1363 in milk was due to deprivation of leucine and methionine.

scholarly journals Transport of -Casein-derived Peptides by the Oligopeptide Transport System Is a Crucial Step in the Proteolytic Pathway ofLactococcus lactis

1995 ◽  
Vol 270 (4) ◽  
pp. 1569-1574 ◽  
Author(s):  
Edmund R. S. Kunji ◽  
Anja Hagting ◽  
Corry J. De Vries ◽  
Vincent Juillard ◽  
Alfred J. Haandrikman ◽  
...  
Keyword(s):  
Transport System ◽  
Crucial Step ◽  
Proteolytic Pathway ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

scholarly journals Utilization of Oligopeptides by Listeria monocytogenes Scott A

1998 ◽  
Vol 64 (3) ◽  
pp. 1059-1065 ◽  
Author(s):  
Annette Verheul ◽  
Frank M. Rombouts ◽  
Tjakko Abee
Keyword(s):  
Listeria Monocytogenes ◽  
Transport System ◽  
Growth Stimulation ◽  
Sole Source ◽  
Fermented Milk ◽  
Defined Medium ◽  
Peptide Transport ◽  
Transport Systems ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

ABSTRACT For effective utilization of peptides, Listeria monocytogenes possesses two different peptide transport systems. The first one is the previously described proton motive force (PMF)-driven di- and tripeptide transport system (A. Verheul, A. Hagting, M.-R. Amezaga, I. R. Booth, F. M. Rombouts, and T. Abee, Appl. Environ. Microbiol. 61:226–233, 1995). The present results reveal that L. monocytogenes possesses an oligopeptide transport system, presumably requiring ATP rather than the PMF as the driving force for translocation. Experiments to determine growth in a defined medium containing peptides of various lengths suggested that the oligopeptide permease transports peptides of up to 8 amino acid residues. Peptidase activities towards several oligopeptides were demonstrated in cell extract from L. monocytogenes, which indicates that upon internalization, the oligopeptides are hydrolyzed to serve as sources of amino acids for growth. The peptide transporters of the nonproteolytic L. monocytogenes might play an important role in foods that harbor indigenous proteinases and/or proteolytic microorganisms, since Pseudomonas fragi as well as Bacillus cereus was found to enhance the growth ofL. monocytogenes to a large extent in a medium in which the milk protein casein was the sole source of nitrogen. In addition, growth stimulation was elicited in this medium when casein was hydrolyzed by using purified protease from Bacillus licheniformis. The possible contribution of the oligopeptide transport system in the establishment of high numbers of L. monocytogenes cells in fermented milk products is discussed.

The identification of oppA gene homologues as part of the oligopeptide transport system in mycoplasmas

Gene ◽  
2015 ◽  
Vol 558 (1) ◽  
pp. 31-40 ◽  
Author(s):  
Martha Wium ◽  
Annelise Botes ◽  
Dirk U. Bellstedt
Keyword(s):  
Transport System ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

Loss of Plasmid-Mediated Oligopeptide Transport System in Lactococci: Another Reason for Slow Milk Coagulation

Plasmid ◽  
1996 ◽  
Vol 35 (3) ◽  
pp. 145-155 ◽  
Author(s):  
Weizhu Yu ◽  
Kevin Gillies ◽  
Jeffery K. Kondo ◽  
Jeffery R. Broadbent ◽  
Larry L. McKay
Keyword(s):  
Transport System ◽  
Milk Coagulation ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

scholarly journals Spontaneous kanamycin-resistant Escherichia coli mutant with altered periplasmic oligopeptide permease protein (OppA) and impermeability to aminoglycosides

1999 ◽  
Vol 30 (2) ◽  
pp. 153-156 ◽  
Author(s):  
Mônica B. Rodriguez ◽  
Sérgio O. P. Costa
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
Cross Resistance ◽  
Bacterial Adaptation ◽  
Coli Mutant ◽  
Oligopeptide Permease ◽  
Permeability Alteration ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

A spontaneous kanamycin-resistant Escherichia coli mutant, showing cross resistance to five other aminoglycosides and absence of the OppA protein was isolated. [3H]-dihydrostreptomycin uptake is reduced in this mutant, implying that the oligopeptide transport system is involved in accumulation of aminoglycosides, although apparently not related with aminoglycoside permeability alteration due to bacterial adaptation to osmotic changes.

Enhancement of the small intestinal uptake of phenylalanyl-glycine via a H+/oligopeptide transport system by chemical modification with fatty acids

Life Sciences ◽  
1997 ◽  
Vol 61 (25) ◽  
pp. 2455-2465 ◽  
Author(s):  
Takuya Fujita ◽  
Yutaka Morishita ◽  
Hitomi Ito ◽  
Daisuke Kuribayashi ◽  
Akira Yamamoto ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Chemical Modification ◽  
Transport System ◽  
Intestinal Uptake ◽  
Small Intestinal ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport
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