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  Tryptophan synthase, an allosteric molecular factory

Barends, T., Dunn, M. F., & Schlichting, I. (2008). Tryptophan synthase, an allosteric molecular factory. Current Opinion in Chemical Biology, 12(5), 593-600. doi:10.1016/j.cbpa.2008.07.011.

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CurrOpinChemicalBiol_12_2008_593.pdf (Any fulltext), 3MB
 
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Barends, Thomas1, Author           
Dunn, Michael F., Author
Schlichting, Ilme1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Tryptophan synthase (TrpS) is a pyridoxal phosphate-containing bifunctional enzyme that catalyzes the last two steps in the biosynthesis of L-tryptophan. Indole, an intermediate generated at the active site of the alpha-subunit is channeled via a 25 A long tunnel to the beta-active site where it reacts with an aminoacrylate intermediate derived from L-serine. The two reactions are kept in phase by allosteric interactions between the two subunits. The recent development of novel alpha-site ligands and alpha-reaction transition state analogs combined with kinetic and crystal structure analysis of Salmonella typhimurium tryptophan synthase has provided new insights into the allosteric regulation of substrate channeling, the reaction mechanisms of the alpha and beta active sites, and the influence of structural dynamics.

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Language(s): eng - English
 Dates: 2008-10-01
 Publication Status: Issued
 Pages: 8
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 Table of Contents: -
 Rev. Type: Peer
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Title: Current Opinion in Chemical Biology
  Other : Curr. Opin. Chem. Biol.
Source Genre: Journal
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Publ. Info: London : Elsevier Current Trends
Pages: - Volume / Issue: 12 (5) Sequence Number: - Start / End Page: 593 - 600 Identifier: ISSN: 1367-5931
CoNE: https://pure.mpg.de/cone/journals/resource/954925620166