8TF7

Apo structure of protein crystal of Tri17

8TF7 の概要

• エントリーDOI: 10.2210/pdb8tf7/pdb
• 分子名称: AMP-binding protein (2 entities in total)
• 機能のキーワード: acyl-coa ligase, amp-binding domain, n-n bond formation, apo structure, ligase
• 由来する生物種: Streptomyces tsukubensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123757.98

構造登録者

Zhai, R.,Zhang, W. (登録日: 2023-07-09, 公開日: 2024-07-10, 最終更新日: 2024-12-11)

主引用文献

Del Rio Flores, A.,Zhai, R.,Kastner, D.W.,Seshadri, K.,Yang, S.,De Matias, K.,Shen, Y.,Cai, W.,Narayanamoorthy, M.,Do, N.B.,Xue, Z.,Marzooqi, D.A.,Kulik, H.J.,Zhang, W.
Enzymatic synthesis of azide by a promiscuous N-nitrosylase.
Nat.Chem., 16:2066-2075, 2024

PubMed Abstract: Azides are energy-rich compounds with diverse representation in a broad range of scientific disciplines, including material science, synthetic chemistry, pharmaceutical science and chemical biology. Despite ubiquitous usage of the azido group, the underlying biosynthetic pathways for its formation remain largely unknown. Here we report the characterization of an enzymatic route for de novo azide construction. We demonstrate that Tri17, a promiscuous ATP- and nitrite-dependent enzyme, catalyses organic azide synthesis through sequential N-nitrosation and dehydration of aryl hydrazines. Through biochemical, structural and computational analyses, we further propose a plausible molecular mechanism for azide synthesis that sets the stage for future biocatalytic applications and biosynthetic pathway engineering.

PubMed: 39333393
DOI: 10.1038/s41557-024-01646-2

実験手法

X-RAY DIFFRACTION (2.45 Å)