8AFU

DaArgC - N-acetyl-gamma-glutamyl-phosphate Reductase of Denitrovibrio acetiphilus

8AFU の概要

• エントリーDOI: 10.2210/pdb8afu/pdb
• 分子名称: N-acetyl-gamma-glutamyl-phosphate reductase, SODIUM ION (3 entities in total)
• 機能のキーワード: formyl-phosphate, oxidoreductase
• 由来する生物種: Denitrovibrio acetiphilus DSM 12809
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78403.47

構造登録者

Pfister, P.,Nattermann, M.,Zarzycki, J.,Erb, T.J. (登録日: 2022-07-18, 公開日: 2023-04-05, 最終更新日: 2024-10-23)

主引用文献

Nattermann, M.,Wenk, S.,Pfister, P.,He, H.,Lee, S.H.,Szymanski, W.,Guntermann, N.,Zhu, F.,Nickel, L.,Wallner, C.,Zarzycki, J.,Paczia, N.,Gaissert, N.,Francio, G.,Leitner, W.,Gonzalez, R.,Erb, T.J.
Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo.
Nat Commun, 14:2682-2682, 2023

PubMed Abstract: Formate can be envisioned at the core of a carbon-neutral bioeconomy, where it is produced from CO by (electro-)chemical means and converted into value-added products by enzymatic cascades or engineered microbes. A key step in expanding synthetic formate assimilation is its thermodynamically challenging reduction to formaldehyde. Here, we develop a two-enzyme route in which formate is activated to formyl phosphate and subsequently reduced to formaldehyde. Exploiting the promiscuity of acetate kinase and N-acetyl-γ-glutamyl phosphate reductase, we demonstrate this phosphate (P)-based route in vitro and in vivo. We further engineer a formyl phosphate reductase variant with improved formyl phosphate conversion in vivo by suppressing cross-talk with native metabolism and interface the P route with a recently developed formaldehyde assimilation pathway to enable C2 compound formation from formate as the sole carbon source in Escherichia coli. The P route therefore offers a potent tool in expanding the landscape of synthetic formate assimilation.

PubMed: 37160875
DOI: 10.1038/s41467-023-38072-w

実験手法

X-RAY DIFFRACTION (1.99 Å)