2VUN
The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily
Summary for 2VUN
| Entry DOI | 10.2210/pdb2vun/pdb |
| Descriptor | ENAMIDASE, ZINC ION, FE (III) ION, ... (6 entities in total) |
| Functional Keywords | nicotinate degradation, binuclear metal center, amidohydrolases, stereospecificity, hydrolase |
| Biological source | EUBACTERIUM BARKERI |
| Total number of polymer chains | 4 |
| Total formula weight | 160949.88 |
| Authors | Kress, D.,Alhapel, A.,Pierik, A.J.,Essen, L.-O. (deposition date: 2008-05-27, release date: 2008-12-09, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 18805424DOI: 10.1016/J.JMB.2008.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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