1LK9
The Three-dimensional Structure of Alliinase from Garlic
1LK9 の概要
| エントリーDOI | 10.2210/pdb1lk9/pdb |
| 分子名称 | ALLIIN LYASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| 機能のキーワード | egf-like domain, plp type 1, chloride binding, lyase |
| 由来する生物種 | Allium sativum (garlic) |
| 細胞内の位置 | Vacuole: Q01594 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 107167.36 |
| 構造登録者 | |
| 主引用文献 | Kuettner, E.B.,Hilgenfeld, R.,Weiss, M.S. The active principle of garlic at atomic resolution J.Biol.Chem., 277:46402-46407, 2002 Cited by PubMed Abstract: Despite the fact that many cultures around the world value and utilize garlic as a fundamental component of their cuisine as well as of their medicine cabinets, relatively little is known about the plant's protein configuration that is responsible for the specific properties of garlic. Here, we report the three-dimensional structure of the garlic enzyme alliinase at 1.5 A resolution. Alliinase constitutes the major protein component in garlic bulbs, and it is able to cleave carbon-sulfur bonds. The active enzyme is a pyridoxal-5'-phosphate-dependent homodimeric glycoprotein and belongs to the class I family of pyridoxal-5'-phosphate-dependent enzymes. In addition, it contains a novel epidermal growth factor-like domain that makes it unique among all pyridoxal-5'-phosphate-dependent enzymes. PubMed: 12235163DOI: 10.1074/jbc.M208669200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.53 Å) |
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