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1 ferase domain by the potent substrate analog moenomycin.
2 r natural products, including the antibiotic moenomycin.
3 nsitive to the glycosyltransferase inhibitor moenomycin.
4 fluorescence on reaction of the protein with moenomycin.
5 ted by the amphiphilic glycolipid antibiotic moenomycin.
6 e observed diversity of terminally decorated moenomycins.
7 ynthesis of the phosphoglycolipid antibiotic moenomycin A attracts the attention of researchers hopin
8                                              Moenomycin A exposure of strain MW2 produced an increase
9                       The natural antibiotic moenomycin A is the prototype for compounds that bind to
10                MGT activity was inhibited by moenomycin A, and the reaction product was sensitive to
11 late steps in cell wall biosynthesis such as moenomycin A, bacitracin and ramoplanin were not inducer
12 doglycan biosynthesis, including ramoplanin, moenomycin A, bacitracin, several glycopeptides and some
13 ot the other mutants, were more sensitive to moenomycin, a transglycosylase inhibitor.
14 LiaRS two-component regulatory system, while moenomycin almost exclusively induces genes that are par
15  Mutants lacking YabM exhibit sensitivity to moenomycin, an antibiotic that blocks peptidoglycan poly
16            In this study, we show that using moenomycin and other glycosyltransferase inhibitors as t
17 etermined by competition experiments between moenomycin and the chromophoric beta-lactam nitrocefin.
18        Moreover, the inhibition constants of moenomycin and two previously identified small molecules
19 synthetic genes involved in the synthesis of moenomycin and variants.
20                                          The moenomycins are phosphoglycolipid antibiotics produced b
21 oli penicillin-binding protein 1b (PBP1b) by moenomycin as well as by various glycopeptides.
22 the target of the pentasaccharide antibiotic moenomycin as well as the proposed target of certain gly
23 fluorescently labeled, truncated analogue of moenomycin based on the minimal pharmacophore.
24 tention of researchers hoping to develop new moenomycin-based antibiotics against multidrug resistant
25 he growing glycan chain (where the inhibitor moenomycin binds) and an acceptor site for lipid II subs
26                 We previously identified the moenomycin biosynthetic gene cluster in order to facilit
27 eriments that establish functions for the 17 moenomycin biosynthetic genes involved in the synthesis
28 s inhibited by the antibiotics, diumycin and moenomycin, but not by a number of other antibiotics or
29                                       At low moenomycin concentration (<20 microM) little inhibition
30 ition of acylation by nitrocefin varied with moenomycin concentration in a biphasic fashion.
31     The variation of this rate constant with moenomycin concentration was consistent with reaction of
32 ions a linear increase in rate constant with moenomycin concentration was observed, yielding a second
33 nctional glycosyltransferase in complex with moenomycin in the donor site, provides a direction for a
34 the quadruple-mutant strain was resistant to moenomycin in vivo.
35  did not react in exactly the same manner as moenomycin, indicating some degree of specificity in rea
36 ce protein anchoring, whereas vancomycin and moenomycin, inhibitors of cell wall polymerization into
37 not previously been possible to evaluate how moenomycin inhibits them or to determine whether glycope
38                                          All moenomycin interactions with sPBP2a were reversible, as
39  the MW2 abcA overexpresser, suggesting that moenomycin is a substrate of AbcA.
40                      We have also found that moenomycin is not competitive with respect to the lipid
41 volved in the biosynthesis of the antibiotic moenomycin, is reported.
42          Unfortunately, the lipophilicity of moenomycin leads to unfavourable pharmacokinetic propert
43 d on novel pyranose scaffold chemistry, with moenomycin-like activity, but with improved drug-like pr
44 uded to arise from reaction of sPBP2a with a moenomycin micelle.
45 centration was consistent with reaction of a moenomycin monomer with the protein with a second-order
46 nhibition was concerted with the reaction of moenomycin monomers, although fast premicellar aggregati
47                              Lower limits to moenomycin off-rates and equilibrium dissociation consta
48          Exposure of the wild-type strain to moenomycin resulted in production of a phenotype similar
49          Here, we compare the ramoplanin and moenomycin stimulons in the Gram-positive model organism
50              Two antibiotics, ramoplanin and moenomycin, target this step by binding to the substrate
51 mising lead is the liposaccharide antibiotic moenomycin that inhibits bacterial glycosyltransferases,
52                             Since the cmc of moenomycin under these conditions was shown to be ca. 20
53                  Relative to MW2, the MIC of moenomycin was decreased 8-fold for MW2DeltaabcA and inc
54 imized enzyme binding properties compared to moenomycin, was designed to identify low-micromolar inhi
55             A general scheme for reaction of moenomycin with sPBP2a is proposed.
56 rst-order rate constants for the reaction of moenomycin with sPBP2a leading to inhibition of acylatio
57 rs, although fast premicellar aggregation of moenomycin with the protein also occurred.
58 ds exhibit in vitro inhibition comparable to moenomycin, with low toxicity and good efficacy in sever

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