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Inhibitory properties

Garbapenem P-Lactamase Inhibitors. Carbapenems are another class of natural product P-lactamase inhibitors discovered about the same time as clavulanic acid. Over forty naturally occurring carbapenems have been identified many are potent P-lactamase inhibitors. Garbapenem is the trivial name for the l-a2abicyclo[3.2.0]hept-2-ene ring system (21) shown in Table 3. The synthesis (74), biosynthesis (75), and P-lactamase inhibitory properties (13,14,66) of carbapenems have been reviewed. Carbapenems are often more potent than clavulanic acid and include type I Cephases in the spectmm of inhibition. Table 3 Hsts the available P-lactamase inhibition data. Synergy is frequendy difficult to demonstrate because the compounds are often potent antibacterials. [Pg.49]

Phenazine-l-carboxamide (137) is known as oxychlororaphine and has been isolated from cultures of Pseudomonas chlororaphisit has some limited inhibitory properties, but the inhibitory action of phenazines is generally disappointing. Some phenazine derivatives have insecticidal properties thus, phenazine itself has been found to be toxic to the clothes moth, the Hawaiian beet webworm, the rice weevil and larva of the codling moth, but under trial conditions its toxicity to plant material, as evidenced by severe burning of foliage, was found to be too high to make it of practical value. [Pg.196]

DNA damaging mutagenic, elastogenic and cell-cell communication inhibitory properties of y-oryzanoL . 1 Toxicol Sci. 16 191-202. [Pg.376]

Several modifications of the structure of the azetidinone were made to improve the inhibitory properties. [Pg.376]

Malina, A., Khan, S., Carlson, C. B., Svitkin, Y., Harvey, I., Sonenberg, N., Beal, P. A., and Pelletier, J. (2005). Inhibitory properties of nucleic acid-binding ligands on protein synthesis. FEBS Lett. 579, 79-89. [Pg.330]

B. Konig, T. Fricke, A. Wa/imann, U. Krallmann-Wenzel, and T. K. Lindhorst, y-Mannosvl clusters scaffolded on azamacrocycles Synthesis and inhibitory properties in the adhesion of type 1 fimbriated Escherichia coli to guinea pig erythrocytes, Tetrahedron Lett., 39 (1998) 2307-2310. [Pg.373]

Most of the pesticide biosensors are designed based on the inhibitory property of enzymes. AChE and butyrylcholinesterase (BChE) are widely used in the development of pesticide biosensors [17, 18], Inhibition leads to a decrease in activity, which... [Pg.56]

VRC3375 was selected from among the 1548 compounds prepared based on its strong PDF inhibitory properties, potent antibacterial activity, and... [Pg.199]

Other inhibitors include alginic acid hydroxamates [80], the natural products myricetin galloylglycosides [81], polyaminoglycosides [82] and a number of antidepressant drugs [83] which demonstrate various degree of SSAO/VAP-1 inhibitory property in rats, humans and cows. [Pg.240]

In addition to the 2 nm shift in the absorption maximum, the two cytochromes can be distinguished by the use of ethyl isocyanide interaction spectra (6, 7) and various inhibitors of the monooxygenase activity (Figure 2 and Table III). The relative magnitude of the ethyl isocyanide-cytochrome P-1+50 interaction spectral peaks at —1+30 and —1+55 nm is pH dependent (6j and if the absorbance differences are plotted as functions of pH, there is a cross-over point at a certain pH which is characteristic for a particular form of cytochrome P-1+50 pH 6.9 for cytochrome P-1+1+8 and pH 7-5-7.6 for PB induced or control cytochrome P-1+50 (6, 21). The cytochrome P-1+50 of apparently uninduced trout species (Salmo trutta lacustris) has been shown by us to have the pH cross-over point for ethyl isocyanide interaction spectrum at pH 7.8 (2l) and the absorption maximum of the reduced trout liver cytochrome P-1+50. 00 complex is 1+50 nm, nevertheless its catalytic and inhibitory properties (2l)(Table III) are similar to those of cytochrome P-1+1+8. [Pg.283]

Some cephalosporins can be both substrates and inhibitors of /3-lactamases. The acyl-enzyme intermediate can undergo either rapid deacylation (Fig. 5.4, Pathway a) or elimination of the leaving group at the 3 -position to yield a second acyl-enzyme derivative (Fig. 5.4, Pathway b), which hydrolyzes very slowly [35][53], Thus, cephalosporins inactivate /3-lactamases by a mechanism similar to that described above for class-II inhibitors. It has been hypothesized that differences in the rate of deacylation of the acyl-enzyme intermediates derive from their different abilities to form H-bonds. A H-bond to NH in Fig. 5.4, Pathway a, may be necessary to assure a catalytically essential conformation of the enzyme, whereas the presence of a H-bond acceptor in Fig. 5.4, Pathway b, may drive the enzyme to an unproductive conformation. The ratio between hydrolysis and elimination, and, consequently, the relative importance of substrate and inhibitor behaviors of cephalosporins, is determined by the nature of the leaving group at C(3 ). An appropriate substitution at C(3 ) of cephalosporins may, therefore, increase the /3-lactamase inhibitory properties and yield potentially better antibiotics [53]. [Pg.194]

In a process environment, the probes must neither corrode nor display catalytic or inhibitory properties. Quinn et al. report that about 30 reactions were run and five different types of metal probes were utilized with a highly corrosive reaction mixture before a custom built PEEK (polyether ether ketone) probe yielded... [Pg.91]


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See also in sourсe #XX -- [ Pg.308 ]




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