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1 port, are catalyzed by lumazine synthase and riboflavin synthase.
2 umazine synthase as well as Escherichia coli riboflavin synthase.
3 itive contribution to its binding to E. coli riboflavin synthase.
4 n an inhibitor of both lumazine synthase and riboflavin synthase.
5 umazine synthase as well as Escherichia coli riboflavin synthase.
6 tilis lumazine synthase and Escherichia coli riboflavin synthase.
7 ine synthase, but it was less potent against riboflavin synthase.
8 ivity for inhibition of lumazine synthase vs riboflavin synthase.
9 e synthase, LovB, macrophomate synthase, and riboflavin synthase.
10 obacterium tuberculosis and Escherichia coli riboflavin synthases.
11 t also forms cage complexes with the cognate riboflavin synthase (AaRS) when both proteins are co-pro
13 sized as inhibitors of both Escherichia coli riboflavin synthase and Bacillus subtilis lumazine synth
17 ad a k(is) of 8.7 microM vs. M. tuberculosis riboflavin synthase and moderate antibiotic activity aga
18 , the amide-containing derivatives inhibited riboflavin synthase and were only very weak or inactive
19 ncluded both the alpha- and beta-subunits of riboflavin synthase as well as a bifunctional enzyme con
20 s subtilis (BsLS), for example, encapsulates riboflavin synthase (BsRS), enabling channeling of lumaz
24 nthase-catalyzed reaction and product of the riboflavin synthase-catalyzed reaction was designed.
27 deling of one of the inhibitors with E. coli riboflavin synthase demonstrated that the active site of
29 For example, the IS-mediated inactivation of riboflavin synthase in COM1 resulted in a riboflavin req
30 its analogues provide the first examples of riboflavin synthase inhibitors with antibiotic activity.
31 nding O-nucleosides as lumazine synthase and riboflavin synthase inhibitors, while the C-nucleosides
32 ly potent inhibitor of both Escherichia coli riboflavin synthase (K(i) 0.61 microM) and Bacillus subt
33 2.7 microM), and Mycobacterium tuberculosis riboflavin synthase (Ki 0.56 muM), while compound 15 is
35 ne synthase (Ki 11 microM), Escherichia coli riboflavin synthase (Ki 2.7 microM), and Mycobacterium t
36 is lumazine synthase (Ki 31 microM), E. coli riboflavin synthase (Ki 47 microM), and M. tuberculosis
37 ds were tested against lumazine synthase and riboflavin synthase obtained from a variety of microorga
38 ested as inhibitors of lumazine synthase and riboflavin synthase obtained from a variety of microorga
39 zine synthase inhibitors and did not inhibit riboflavin synthase, the amide-containing derivatives in
40 s led to inhibition of lumazine synthase and riboflavin synthase when combined with the replacement o
41 olumazine (15) in the active site of E. coli riboflavin synthase, which demonstrated that the active
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