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Sugar aureus

The main function of the ester 34 in bacterial cells seems to be its participation in the biosynthesis of the glycopeptide cell-wall polymer. If this process is blocked, there results the accumulation of a high concentration of sugar nucleotide precursors in the cell. A number of these compounds have been isolated the simplest one is the ester of uridine 5 -pyrophosphate with N-acetylmuramic acid [2-acetamido-3-0-(D-l-carboxyethyl)-2-deoxy-D-glucose] (37), first obtained from Staphylococcus aureus cells that had been treated with penicillin7,151 or Gentian Violet.144 An intermediate in the biosynthesis of 37 was isolated and shown to be the 3 -enolpyruvate ether152,153 (38). [Pg.328]

Kennedy, E. P. and Scarborough, G. A. 1967. Mechanism of hydrolysis of O-nitrophenyl-d-galactoside in Staphylococcus aureus and its significance for theories of sugar transport. Proc. Natl. Acad. Sci. USA 58, 225-228. [Pg.728]

The polyprenols obtained from tobacco and Arum maculatum (solanesol and spadicol), which are all E, are the exceptions. Another interesting fact is that, in most seed-plants, the polyprenols are allylic, as is bacterial undecaprenol. Saturated or slightly modified polyprenols, such as animal dolichol, seem to be present only in fungi. Any of those plant polyprenols, in a phosphorylated form, can be potential sugar acceptors for transfer reactions. Experiments were performed with phosphorylated allylic polyprenols and membrane preparations from Phaseolus aureus. D-Mannose from GDP-D-mannose was incorporated into the exogenous, polyprenyl phosphates,29,49 52 but it was not possible to establish unequivocally the role of these polyprenols as lipid intermediates. [Pg.349]

The class of sugars or carbohydrates that contains one unit of the sugar. It is the simplest class of sugars, e.g. C6Hi2C>6, glucose. Methicillin-resistant Staphylococcus aureus (MRSA). Often called the hospital superbug because it is resistant to most of penicillin treatments. [Pg.247]

Plasmid-mediated resistance to QACs and chlorhexidine in S. aureus has been cloned in E. coli [302] but the level of resistance is low and the mechanism not fully elucidated. The efflux-mediated antiseptic resistance gene qacA from S. aureus has a common ancestry with tetracycline- and sugar-transported proteins [227-229]. [Pg.182]

The Lipid I and II building blocks may be further elaborated by many other enzymes that modify the sugars or amino acid chains. Branched peptides are added to the Lipid I and II peptide chains either by enzymes that act in an ATP-dependent fashion similar to the MurC-F ligases [39], or by enzymes that add amino acid residues from aminoacyl tRNA intermediates, such as the S. aureus enzymes FemA, FemB and FemX, which form the pentaglycine bridge (O Fig. 3) [36], and the S. pneumoniae enzymes FemM and FemN, which form an L-Ser-L-Ala or L-Ala-L-Ala dipeptide bridge [34,35]. Lipid II is also the substrate for the sortase enzymes that catalyze the attachment of surface proteins for incorporation into peptidoglycan [40]. [Pg.1545]

In this investigation, three main focus areas are reported (1) S. aureus growth in homogeneous liquid media system, (2) mold spore germination in heterogeneous semi-solid starch-sugars and cellulose-sorbose systems with, and (3) survival of organisms in freeze-dried locust bean and xanthan... [Pg.170]

Yamaguchi T, Hayashi T, Takami H, Nakasone K, Ohnishi M, Nakayama K, Yamada S, Komatsuzawa H, Sugar M (2000) Phage conversion of exfoliative toxin A production in Staphylococcus aureus. Mol Microbiol 38 694-705 Yamaguchi T, Hayashi T, Takami H, Ohnishi M, Murata T, Nakayama K, Asakawa K, Ohara M, Komatsuzawa H, Sugai M (2001) Complete nucleotide sequence of a Staphylococcus aureus exfoliative toxin B plasmid and identification of a novel ADP-ribosyltransferase, EDIN-C. Infect Immun 69 7760-7771... [Pg.183]


See other pages where Sugar aureus is mentioned: [Pg.164]    [Pg.112]    [Pg.526]    [Pg.100]    [Pg.308]    [Pg.234]    [Pg.660]    [Pg.328]    [Pg.369]    [Pg.370]    [Pg.353]    [Pg.275]    [Pg.140]    [Pg.142]    [Pg.146]    [Pg.369]    [Pg.373]    [Pg.367]    [Pg.1065]    [Pg.43]    [Pg.176]    [Pg.206]    [Pg.207]    [Pg.208]    [Pg.209]    [Pg.294]    [Pg.95]    [Pg.339]    [Pg.713]    [Pg.105]    [Pg.164]    [Pg.2554]    [Pg.402]    [Pg.9]    [Pg.12]    [Pg.312]    [Pg.233]    [Pg.233]    [Pg.191]    [Pg.31]   
See also in sourсe #XX -- [ Pg.369 , Pg.371 ]




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