Escherichia coii activation

Class Synthetic antibacterial combinations with activity against Escherichia coii, Pro/eos species. Morganeiia morganii, Proteus mirahiiis, Kiebsielia species. Enterobacterspecies, Hemophiius influenzae, Streptococcus pneumoniae, Shigella flexneri, and Shigella sonnei 15 o u E c... 

Class Semisynthetic aminoglycoside antibiotics with activity against Pseudomonas species, Escherichia coii. Proteus species, Providencia species, Klebsiella species, Enterobacter speaes, Serratia species, Acinetobacter species, Citrobacter freundii, Staphylococcus species Aminoglycosides generally have a low level of activity against grampositive organisms Lo o u c <... 

Mohn. G. R.. Vogels-Bouter, S. van der Horst-van der Zon, J. (1981) Studies on the mutagenic activity of 20 coded compounds in liquid tests using the multipurpose strain Escherichia coii K-122/343/113 and derivatives. In de Serres, F.J. Ashby. J., eds. Evaluation of Short-Term Tests for Carcinogens. Report of the International Collaborative Program (Progress in Mutation Research, Vol. 1), Amsterdam, Elsevier, pp. 396-413... 

Fig. 1. The active sites of PT SI and of the A subunits of diphtheria toxin and Escherichia coii heat labile toxin. The thin lines represent the carbon backbones. Only those (3 strands and a helices that are relevant for the active-site geometry are shown. The side chains of residues involved in the enzyme activity, especially those of the catalytic Glu and His residues, are represented by the thick lines. The a2 helix present in PT (top) and coii heat labile toxin (LT, right) is completely missing in diphtheria toxin (DT, left)...

Figure 27 Active-site residues of SADH that interact with the guanidine of the substrate, N -succinylarginine (33) (shown in blue). Core residues are shown in black and a neighboring Glu in gray. N110 is found in the same position as the lateral Asp residues of ADI, and D250 serves as the anterior Asp. Amino acid numbering is taken from the Escherichia coii SADH protein.

Beacham, I.R., Kahana, R., Levy, L. and Yagil, E. (1 973) Mutants of Escherichia coii K-12 cryptic, or deficient in 5 -nucleotidase (uridine diphosphate-sugar hydrolase) and 3 -nucleotidase (cyclic phosphodiesterase) activity.yourna/ of Bacterioiogy 11 5, 957-964. 

Active against Bacillus subtilis, Pseudomonas species, Escherichia coii, Staphylococcus species, fungi, algae and yeasts... 

TABLE XXVI Effect of 7a-Methoxy Substitution of Cefuroxime, Cephamandole, Cephapirin, and Cephalosporin 87/359 upon Inhibition of Membrane-bound Model Transpeptidase Activity of Escherichia coii DCO"... 

Figure 17.10 Metabolic pathways involved in SA production in the metabolically engineered Escherichia coii SBS550MG strain. NADH competing pathways are knocked out with the knockout of acetate pathway, while glyoxylate shunt is activated by knockout of the icIR with introduction of the Lactococcus lactis pyc gene. Black lines indicate overexpression. X indicate knocked out genes. PEP, phosphoenolpyruvate OAA, oxaloac-etate MAL, malate FUM, fumarate Suc-CoA, succinyl-CoA a-KG, a-ketoglutarate ICT, isocitrate CIT, citrate PYR, pyruvate AcCoA, acetyl-CoA idhA, lactate dehydrogenase pta,...

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