2VUN

The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily

2VUN の概要

• エントリーDOI: 10.2210/pdb2vun/pdb
• 分子名称: ENAMIDASE, ZINC ION, FE (III) ION, ... (6 entities in total)
• 機能のキーワード: nicotinate degradation, binuclear metal center, amidohydrolases, stereospecificity, hydrolase
• 由来する生物種: EUBACTERIUM BARKERI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160949.88

構造登録者

Kress, D.,Alhapel, A.,Pierik, A.J.,Essen, L.-O. (登録日: 2008-05-27, 公開日: 2008-12-09, 最終更新日: 2024-05-08)

主引用文献

Kress, D.,Alhapel, A.,Pierik, A.J.,Essen, L.-O.
The Crystal Structure of Enamidase: A Bifunctional Enzyme of the Nicotinate Catabolism.
J.Mol.Biol., 384:837-, 2008

PubMed Abstract: The hydrolysis of 1,4,5,6-tetrahydro-6-oxonicotinate to 2-formylglutarate is a central step in the catabolism of nicotinate in several Clostridia and Proteobacteria. This reaction is catalyzed by the novel enzyme enamidase, a new member of the amidohydrolase superfamily as indicated by its unique reaction, sequence relationship, and the stoichiometric binding of iron and zinc. A hallmark of enamidase is its capability to catalyze a two-step reaction: the initial decyclization of 1,4,5,6-tetrahydro-6-oxonicotinate leading to 2-(enamine)glutarate followed by an additional hydrolysis step yielding (S)-2-formylglutarate. Here, we present the crystal structure of enamidase from Eubacterium barkeri at 1.9 A resolution, providing a structural basis for catalysis and suggesting a mechanism for its exceptional activity and enantioselectivity. The enzyme forms a 222-symmetric tetramer built up by a dimer of dimers. Each enamidase monomer consists of a composite beta-sandwich domain and an (alpha/beta)(8)-TIM-barrel domain harboring the active site. With its catalytic binuclear metal center comprising both zinc and iron ions, enamidase represents a special case of subtype II amidohydrolases.

PubMed: 18805424
DOI: 10.1016/J.JMB.2008.09.002

実験手法

X-RAY DIFFRACTION (1.89 Å)