Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis

Fujishiro, Takashi; Tamura, Haruka; Schick, Michael; Kahnt, Jörg; Xie, Xiulan; Ermler, Ulrich; Shima, Seigo

doi:10.1002/anie.201306745

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

Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis

MPS-Authors

/persons/resource/persons137648

Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource

There are no locators available

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

Fujishiro, T., Tamura, H., Schick, M., Kahnt, J., Xie, X., Ermler, U., & Shima, S. (2013). Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis. Angewandte Chemie, International Edition in English, 52(48), 12555-12558. doi:10.1002/anie.201306745.

引用: https://hdl.handle.net/11858/00-001M-0000-0024-D492-8

要旨

One reaction step of the biosynthesis of [Fe]-hydrogenase-cofactor is elucidated by S. Shima et al. in their Communication on page 12555 ff. A structural genomics approach, in combination with model reactions and thorough product analysis by X-ray crystallography of the protein–product complexes, revealed that HcgB is the enzyme that catalyzes guanylylpyridinol formation from a 2,4-dihydroxypyridine derivative and guanosine triphosphate.