4S13
Ferulic Acid Decarboxylase (FDC1)
4S13 の概要
| エントリーDOI | 10.2210/pdb4s13/pdb |
| 分子名称 | Ferulic acid decarboxylase 1, 4-ethenylphenol (3 entities in total) |
| 機能のキーワード | decarboxylase, lyase |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) |
| 細胞内の位置 | Cytoplasm : Q03034 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 450454.15 |
| 構造登録者 | |
| 主引用文献 | Bhuiya, M.W.,Lee, S.G.,Jez, J.M.,Yu, O. Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae. Appl.Environ.Microbiol., 81:4216-4223, 2015 Cited by PubMed Abstract: The nonoxidative decarboxylation of aromatic acids occurs in a range of microbes and is of interest for bioprocessing and metabolic engineering. Although phenolic acid decarboxylases provide useful tools for bioindustrial applications, the molecular bases for how these enzymes function are only beginning to be examined. Here we present the 2.35-Å-resolution X-ray crystal structure of the ferulic acid decarboxylase (FDC1; UbiD) from Saccharomyces cerevisiae. FDC1 shares structural similarity with the UbiD family of enzymes that are involved in ubiquinone biosynthesis. The position of 4-vinylphenol, the product of p-coumaric acid decarboxylation, in the structure identifies a large hydrophobic cavity as the active site. Differences in the β2e-α5 loop of chains in the crystal structure suggest that the conformational flexibility of this loop allows access to the active site. The structure also implicates Glu285 as the general base in the nonoxidative decarboxylation reaction catalyzed by FDC1. Biochemical analysis showed a loss of enzymatic activity in the E285A mutant. Modeling of 3-methoxy-4-hydroxy-5-decaprenylbenzoate, a partial structure of the physiological UbiD substrate, in the binding site suggests that an ∼30-Å-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail of the substrate needed for ubiquinone biosynthesis in yeast. The three-dimensional structure of yeast FDC1 provides a template for guiding protein engineering studies aimed at optimizing the efficiency of aromatic acid decarboxylation reactions in bioindustrial applications. PubMed: 25862228DOI: 10.1128/AEM.00762-15 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.348 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






