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Escherichia coli activation

Escherichia coli Diarrhoea-producing Escherichia coli Activates C-type PM GC... [Pg.262]

Hong, S.H., Ntai, I., Haimovich, A.D., Kelleher, N.L. et al. (2014) Cell-free protein synthesis from a release factor 1 deficient Escherichia coli activates efficient and multiple site-specific nonstandard amino acid incorporation. [Pg.817]

Specific bacteriostatic activity against Escherichia coli (681, 896, 899), Staphylococcus aureus (681, 896), Cocci (900), Shigella dysenteriae (681), Salmonella ryphi (681), Proteus vulgaris (681), Pseudomonas aeruginosa (681), Streptococcus (889, 901, 902) and Pneumococcus (901-904). [Pg.152]

Sulfaphenazole (684) and sulfazamet (685) are both examples of relatively short acting sulfonamides (B-80MI40406) and their antibacterial activity has been tested against Escherichia coli, the former being more effective than the latter. Sulfaphenazole also displaces sulfonyl ureas from protein binding sites on human serum albumin and consequently increases the concentration of the free (active) drug and produces a more intense reaction that may result in hypoglycemia. [Pg.291]

The trp repressor controls the operon for the synthesis of L-tryptophan in Escherichia coli by a simple negative feedback loop. In the absence of L-tryptophan, the repressor is inactive, the operon is switched on and the enzymes which synthesize L-tryptophan are produced. As the concentration of L-tryptophan increases, it binds to the repressor and converts it to an active form so that it can bind to the operator region and switch off the gene. [Pg.142]

Condensation of 165 with chloroacetamide derivatives afforded (89JIC246) carbamoylhydrazino derivatives 168. Some are active against S. aureus and Escherichia coli. Condensation of 165 with ethyl cyanoace-tate, malononitrile, ethyl acetoacetate, or acetylacetone gave (87AP1191, 87PHA664 89JHC769) 169 and 170, whose bactericidal activity has been reported. [Pg.60]

L-aspartic add has been produced on an industrial scale by the Tanabe Seiyaku Co Ltd, Japan, in a batch wise process using whole cells of Escherichia coli with high aspartase activity. In this process, L-aspartic add is produced from fumaric add and ammonia using aspartase, as described in Figure A8.13. [Pg.287]

Since 1978, several papers have examined the potential of using immobilised cells in fuel production. Microbial cells are used advantageously for industrial purposes, such as Escherichia coli for the continuous production of L-aspartic acid from ammonium fur-marate.5,6 Enzymes from microorganisms are classified as extracellular and intracellular. If whole microbial cells can be immobilised directly, procedures for extraction and purification can be omitted and the loss of intracellular enzyme activity can be kept to a minimum. Whole cells are used as a solid catalyst when they are immobilised onto a solid support. [Pg.200]

Escherichia coli Adenine and adenosine are inhibitory74 and the synthesis of thiamine can be derepressed by culture in their presence.13,75 adth- Mutants are known.76 [l4C]Formate incorporates at C-2 of pyramine without dilution of molar activity. Glycine labeled with stable isotopes was fed to E. coli and the pyramine was analyzed by mass spectrometry. The two carbon atoms of glycine separated during the biosynthesis. The carboxyl was found12 at C-4, and the C-N fragment was the precursor of C-6-N-1. In conclusion, it is beyond doubt that pyramine synthesis follows the AIR pathway in E. coli. [Pg.305]

Similarly, Ikehara, Tazawa, and Fukui (51) have found that the nucleotides 8-bromo and 8-oxoadenosine 5 -diphosphate, 8-bromo-, 8-oxo, and 8-dimethylaminoguanosine 5 -diphosphate are all inactive as substrates for homopolymer synthesis catalyzed by polynucleotide phosphorylase from Escherichia coli. Some of the results were later confirmed by Kapuler, Monny, and Michelson (52), who found that neither 8-bromo- nor 8-oxoguanosine 5 -diphosphate was active as a substrate for homopolymerization with polynucleotide phosphorylases isolated both irom Azotobacter vinelandii and . coli. [Pg.388]

Escherichia coli K12 TGI strain was used as a recipient for transformation. At studying of SOS-system activity the recombinant bioluminescent strain of Escherichia coli recA lux containing plasmid-borne fusions of the recA promoter-operator region to the Photorhabdus luminescens ZM 1 lux genes (GosNlIgenetika, Russia) was used. Increase of their luminescence in the presence of DNA damage factors [Rosen et al., 2000], were shown previously. Investigation of the luminescent response of this strain to UV radiation allows quantitatively estimate in a real time a SOS-system induction. [Pg.186]


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See also in sourсe #XX -- [ Pg.582 ]

See also in sourсe #XX -- [ Pg.6 , Pg.582 ]




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