Tryptophan synthase, an allosteric molecular factory

Barends, Thomas; Dunn, Michael F.; Schlichting, Ilme

doi:10.1016/j.cbpa.2008.07.011

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

Tryptophan synthase, an allosteric molecular factory

MPS-Authors

/persons/resource/persons92083

Barends, Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://dx.doi.org/10.1016/j.cbpa.2008.07.011
(全文テキスト（全般）)

http://www.sciencedirect.com/science/article/pii/S1367593108001129/pdfft?md5=2a429c9728f5cb46a2029593b039784a&pid=1-s2.0-S1367593108001129-main.pdf
(全文テキスト（全般）)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

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.

引用: https://hdl.handle.net/11858/00-001M-0000-0028-79F1-5

要旨

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.