Disease relevance of Enterococcus faecium

• The peptides produced by cleavage of the S-cyano derivatives of the ornithine transcarbamylases (ornithine carbamoyltransferase, 2.1.3.3) from bovine liver, Streptococcus faecalis ATCC 11,420, and Streptococcus faecium ATCC 8043 have been isolated and aligned [1].
• The antifolate activity was evaluated with methotrexate (MTX) sensitive and MTX-resistant strains of Lactobacillus casei and Streptococcus faecium [2].
• The chicken liver enzyme is homologous to that from L1210 cells and shows regions of homology to dihydrofolate reductases from Streptococcus faecium, Escherichia coli, and Lactobacillus casei [3].
• The in vitro growth of Streptococcus mutans was completely inhibited by water-soluble extracts from cells of various intestinal lactic acid bacteria identified as Streptococcus faecium, Streptococcus equinus, Lactobacillus fermentum, and Lactobacillus salivarius [4].
• Previously, 8-deazafolic acid (17) was shown to be a potent inhibitor of the folate-dependent bacteria, Streptococcus faecium (ATCC 8043) and Lactobacillus casei (ATCC 7469), and to have activity against lymphoid leukemia L1210 in mice [5].

High impact information on Enterococcus faecium

• Covalent modification of the beta-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate [6].
• Association of RNA with thymidylate synthase from methotrexate-resistant Streptococcus faecium [7].
• Thymidylate synthase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45) from methotrexate-resistant Streptococcus faecium has a UV absorbance peak at 259 nm and stains with acridine orange because of the presence of RNA on the protein [7].
• An FAD-containing L-alpha-glycerophosphate oxidase has been purified to homogeneity from Streptococcus faecium [8].
• The action of purified N-acetylmuramoylhydrolase (muramidase, EC 3.2.1.17) of Streptococcus faecium ATCC 9790 on linear, uncross-linked, soluble, peptidoglycan chains produced by the same organism in the presence of benzylpenicillin was characterized as a processive exodisaccharidase [9].

Chemical compound and disease context of Enterococcus faecium

• The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Partial sequence and order of the limited tryptic and cyanogen bromide peptides [10].
• Dodecylglycerol has a minimum inhibitory concentration of 4 micrograms/ml compared to 9 micrograms/ml for monolaurin (dodecanoylglycerol) with Streptococcus faecium ATCC 9790 as the test organism [11].
• Carboxymethylation by iodoacetate of dihydrofolate reductase from the amethopterin-resistant mutant Streptococcus faecium var [12].
• Finally, a cysteine containing hexapeptide (residues 268-273), the putative ornithine binding site in Streptococcus faecalis, Streptococcus faecium, and bovine transcarbamylases, is completely conserved among the two E. coli and the two mammalian transcarbamylases [13].
• Bactericidal activity of five combinations of penicillin G with aminoglycosides against Streptococcus faecium [14].

Biological context of Enterococcus faecium

• The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein [15].

Anatomical context of Enterococcus faecium

• Rutin-induced beta-glucosidase activity in Streptococcus faecium VGH-1 and Streptococcus sp. strain FRP-17 isolated from human feces: formation of the mutagen, quercetin, from rutin [16].
• Two phenotypically autolysis-deficient strains of Streptococcus faecium ATCC 9790 were shown to produce high-molecular-weight, soluble, linear, uncross-linked peptidoglycan when incubated with benzylpenicillin in a wall medium which permits cell wall synthesis (wall thickening) but not balanced growth [17].
• PURPOSE: To investigate the antimicrobial efficacy of a chlorhexidine gluconate (2.0%) and of an ethanolic chloroxylenol solution (10%) as a temporary root canal dressing against selected test microorganisms (Staphylococcus aureus, Streptococcus faecium, Escherichia coli, Candida albicans) [18].

Gene context of Enterococcus faecium

• Identification, cloning and sequence of the Streptococcus faecium infB (translational initiation factor IF2) gene [19].
• In bacterial studies on the 2-amino-4-oxo analogues, 5-deazafolic acid proved to be a potent inhibitor of Lactobacillus casei DHFR and also the growth of both L. casei ATCC 7469 and Streptococcus faecium ATCC 8043 [20].
• Dihydrofolate reductase from the amethopterin-resistant mutant (strain A) of Streptococcus faecium var [21].
• IL-10 production was significantly up-regulated following stimulation with Bifidobacteria longum, but not after exposure to lipopolysaccharide (LPS) or Streptococcus faecium [22].
• The N-terminal sequence of one of them, belonging to class A, showed strong homology with the N-terminal sequence of carbamate kinase from Streptococcus faecium [23].

Analytical, diagnostic and therapeutic context of Enterococcus faecium

• Crystallization, characterization and preliminary crystallographic studies of carbamate kinase of Streptococcus faecium [24].
• Stopped-flow spectrophotometry and stopped-flow fluorometry have been used to study the binding of methotrexate (MTX) and 3-deazamethotrexate (3-deazaMTX) to dihydrofolate reductase (DHFR) isoenzymes from Streptococcus faecium and from Lactobacillus casei [25].

References