Výsledky vyhledávání - "B. M. Chassy"

Genetic engineering of lactobacilli, leuconostocs and Streptococcus thermophilus

Autor: P. H. Pouwels, A. Mercenier, B. M. Chassy

Publikováno v: Genetics and Biotechnology of Lactic Acid Bacteria ISBN: 9789401045841
Gasson, M.Vos, W.M. de, Genetics and biotechnology of lactic acid bacteria, 252-293

The lactic acid bacteria represent a large heterogeneous family of microorganisms that share the property of converting fermentable carbohydrates primarily to lactic acid. The homofermentative lactic acid bacteria convert one mole of glucose to two m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1401ab5249a5e590865f529c0cc355d9
https://doi.org/10.1007/978-94-011-1340-3_6

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Repeated DNA sequence involved in mutations affecting transport of sucrose into Streptococcus mutans V403 via the phosphoenolpyruvate phosphotransferase system

Autor: Kevin R. Jones, S M Michalek, C A Alpert, Francis L. Macrina, B M Chassy

Publikováno v: Infection and immunity. 59(4)

Mutants of Streptococcus mutans V403 defective in the intracellular sucrose-6-phosphate hydrolase (product of the scrB gene) are sensitive to sucrose because of the intracellular accumulation of the phosphorylated sugar. Using a scrB mutant prepared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a55d85b485bb55dc8e23ee65c61578e3
https://pubmed.ncbi.nlm.nih.gov/2004831

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Molecular cloning and DNA sequence of lacE, the gene encoding the lactose-specific enzyme II of the phosphotransferase system of Lactobacillus casei. Evidence that a cysteine residue is essential for sugar phosphorylation

Autor: C A, Alpert, B M, Chassy

Publikováno v: The Journal of biological chemistry. 265(36)

The gene coding for the lactose-specific Enzyme II of the Lactobacillus casei phosphoenolpyruvate-dependent phosphotransferase system, lacE, has been isolated by molecular cloning and expressed in Escherichia coli. The DNA sequence of the lacE gene a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::00c0841abf7d896581e3a0b2397737e6
https://pubmed.ncbi.nlm.nih.gov/2125053

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Intracellular phosphorylation of glucose analogs via the phosphoenolpyruvate: mannose-phosphotransferase system in Streptococcus lactis

Autor: B M Chassy, J Thompson

Publikováno v: Journal of Bacteriology. 162:224-234

The bacterial phosphoenolpyruvate:sugar-phosphotransferase system (PTS) mediates the vectorial translocation and concomitant phosphorylation of sugars. The question arises of whether the PTS can also mediate the phosphorylation of intracellular sugar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3580f478e8020d55aa81effc41b0a863
https://doi.org/10.1128/jb.162.1.224-234.1985

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Regulation of glycolysis and sugar phosphotransferase activities in Streptococcus lactis: growth in the presence of 2-deoxy-D-glucose

Autor: B M Chassy, J Thompson

Publikováno v: Journal of Bacteriology. 154:819-830

Streptococcus lactis K1 has the capacity to grow on many sugars, including sucrose and lactose, in the presence of high levels (greater than 500 mM) of 2-deoxy-D-glucose. Initially, growth of the organism was transiently halted by the addition of com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecd053700471c235e113d9a44e6577cf
https://doi.org/10.1128/jb.154.2.819-830.1983

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Intracellular hexose-6-phosphate:phosphohydrolase from Streptococcus lactis: purification, properties, and function

Autor: J Thompson, B M Chassy

Publikováno v: Journal of Bacteriology. 156:70-80

An intracellular hexose 6-phosphate:phosphohydrolase (EC 3.1.3.2) has been purified from Streptococcus lactis K1. Polyacrylamide disc gel electrophoresis of the purified enzyme revealed one major activity staining protein and one minor inactive band.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a50bbce7373200d96794f9f5537c6fc5
https://doi.org/10.1128/jb.156.1.70-80.1983

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Occurrence and distribution of sucrose-metabolizing enzymes in oral streptococci

Autor: E V Porter, Jacob A. Donkersloot, R M Bielawski, J R Beall, B M Chassy

Publikováno v: Infection and Immunity. 14:408-415

Specific growth rates, growth yields, and the level and cellular distribution of three sucrose-metabolizing enzyme activities were determined for seven oral streptococci (Streptococcus mutans strains E49, BHT, 10449, SL-1, and LM-7, S. sanguis 10558,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92cef0375615ea69e271fc94ac571361
https://doi.org/10.1128/iai.14.2.408-415.1976

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Novel phosphoenolpyruvate-dependent futile cycle in Streptococcus lactis: 2-deoxy-D-glucose uncouples energy production from growth

Autor: J Thompson, B M Chassy

Publikováno v: Journal of Bacteriology. 151:1454-1465

The addition of 2-deoxy-D-glucose to cultures of Streptococcus lactis 133 that were growing exponentially on sucrose or lactose reduced the growth rate by ca. 95%. Inhibition did not occur with glucose or mannose as the growth sugar. The reduction in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd948eae88719bf7b32275c27783fde2
https://doi.org/10.1128/jb.151.3.1454-1465.1982

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Cloning and expression of the beta-D-phosphogalactoside galactohydrolase gene of Lactobacillus casei in Escherichia coli K-12

Autor: B. M. Chassy, E. K. Jagusztyn-Krynicka, L J Lee, J. B. Hansen

Publikováno v: Journal of Bacteriology. 152:1138-1146

Lactose metabolism in Lactobacillus casei 64H is associated with the presence of plasmid pLZ64. This plasmid determines both phosphoenolpyruvate-dependent phosphotransferase uptake of lactose and beta-D-phosphogalactoside galactohydrolase. A shotgun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63a721c8b5bfbfb86844d78089ede9ab
https://doi.org/10.1128/jb.152.3.1138-1146.1982

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