5O3N

Crystal structure of E. cloacae 3,4-dihydroxybenzoic acid decarboxylase (AroY) reconstituted with prFMN

5O3N の概要

• エントリーDOI: 10.2210/pdb5o3n/pdb
• 分子名称: 3,4-dihydroxybenzoate decarboxylase, MANGANESE (II) ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: decarboxylase, prfmn, lyase
• 由来する生物種: Enterobacter cloacae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 113304.25

構造登録者

Marshall, S.A.,Leys, D. (登録日: 2017-05-24, 公開日: 2017-09-13, 最終更新日: 2024-05-08)

主引用文献

Payer, S.E.,Marshall, S.A.,Barland, N.,Sheng, X.,Reiter, T.,Dordic, A.,Steinkellner, G.,Wuensch, C.,Kaltwasser, S.,Fisher, K.,Rigby, S.E.J.,Macheroux, P.,Vonck, J.,Gruber, K.,Faber, K.,Himo, F.,Leys, D.,Pavkov-Keller, T.,Glueck, S.M.
Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase.
Angew. Chem. Int. Ed. Engl., 56:13893-13897, 2017

PubMed Abstract: The utilization of CO as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme-catalyzed para-carboxylation of catechols, employing 3,4-dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirmed that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMN species. This study reports on the in vitro reconstitution and activation of a prFMN-dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving an intermediate with a single covalent bond between a quinoid adduct and cofactor is proposed, which is distinct from the mechanism of prFMN-associated 1,3-dipolar cycloadditions in related enzymes.

PubMed: 28857436
DOI: 10.1002/anie.201708091

実験手法

X-RAY DIFFRACTION (2.05 Å)