期刊論文
| 學年 | 114 |
|---|---|
| 學期 | 1 |
| 出版（發表）日期 | 2025-08-23 |
| 作品名稱 | Enzymatic activity and substrate specificity of recombinant zebrafish D-amino acid oxidase. |
| 作品名稱（其他語言） | |
| 著者 | Ming-Kai Chern; Yun-Hsin Wang; Mei-Yun Huang; I-Ching Kuan; Bo-Chang Wang; Yau-Hung Chen |
| 單位 | |
| 出版者 | |
| 著錄名稱、卷期、頁數 | Asia-Pacific Journal of Molecular Biology and Biotechnology 33(3), p.46-50 |
| 摘要 | D-amino acid oxidase (DAO) is a peroxisomal enzyme that catalyzes the oxidative deamination of D-amino acids. In this study, we employed a bacterial expression system to express and purify a ~38 kDa recombinant zebrafish DAO (zDAO) protein. The kinetic parameters, including Km (μM), Kcat (nmol/min/mg), and substrate specificity (Kcat/Km), were determined. All D-amino acids were tested as substrates. Among them, zDAO exhibited the highest specificity for D-alanine (0.537), making it the preferred substrate. In contrast, D-threonine showed the lowest specificity (0.018), approximately 3% of that for D-alanine. These findings provide further insight into the enzymatic properties of fish DAO. |
| 關鍵字 | Co²⁺-NTA agarose column; D-amino acids; D-amino acid oxidase; zebrafish; flavoenzyme; His-tag |
| 語言 | en |
| ISSN | 0128-7451 |
| 期刊性質 | 國外 |
| 收錄於 | SCI |
| 產學合作 | |
| 通訊作者 | Yau-Hung Chen |
| 審稿制度 | 是 |
| 國別 | MYS |
| 公開徵稿 | |
| 出版型式 | ,電子版 |
| 相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/129591 ) |