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Tryptophan synthase: the workings of a channeling nanomachine.
Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I. Dunn MF, et al. Among authors: niks d. Trends Biochem Sci. 2008 Jun;33(6):254-64. doi: 10.1016/j.tibs.2008.04.008. Epub 2008 May 15. Trends Biochem Sci. 2008. PMID: 18486479 Review.
Allosteric regulation of tryptophan synthase channeling: the internal aldimine probed by trans-3-indole-3'-acrylate binding.
Casino P, Niks D, Ngo H, Pan P, Brzovic P, Blumenstein L, Barends TR, Schlichting I, Dunn MF. Casino P, et al. Among authors: niks d. Biochemistry. 2007 Jul 3;46(26):7728-39. doi: 10.1021/bi700386b. Epub 2007 Jun 9. Biochemistry. 2007. PMID: 17559231
Here we employ the chromophoric l-Trp analogue, trans-3-indole-3'-acrylate (IA), and noncleavable alpha-site ligands (ASLs) to probe the allosteric properties of the internal aldimine, E(Ain). The ASLs studied are alpha-d,l-glycerol phosphate (GP) and d-glyceraldehy …
Here we employ the chromophoric l-Trp analogue, trans-3-indole-3'-acrylate (IA), and noncleavable alpha-site ligands (ASLs) to probe the all …
Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands.
Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF. Ngo H, et al. Among authors: niks d. Biochemistry. 2007 Jul 3;46(26):7740-53. doi: 10.1021/bi7003872. Epub 2007 Jun 9. Biochemistry. 2007. PMID: 17559232
Here, we compare the behavior of new ASLs as allosteric effectors of stage I with the behavior of the natural product, d-glyceraldehyde 3-phosphate. Rapid kinetics and kinetic isotope effects show these ASLs bind with affinities ranging from micro- to millimolar, and the r …
Here, we compare the behavior of new ASLs as allosteric effectors of stage I with the behavior of the natural product, d-glyceraldehy …
50 results