Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate
文献类型：期刊论文
| 作者 | Zeng, Yi-Fang2; Ko, Tzu-Ping5; Lai, Hui-Lin8; Cheng, Ya-Shan2; Wu, Tzu-Hui8; Ma, Yanhe1; Chen, Chun-Chi6; Yang, Chii-Shen4; Cheng, Kuo-Joan8; Huang, Chun-Hsiang1 |
| 刊名 | JOURNAL OF MOLECULAR BIOLOGY
 |
| 出版日期 | 2011-06-03 |
| 卷号 | 409期号:2页码:214-224 |
| 关键词 | myo-inositol hexasulfate phytate phytase crystal structure synchrotron radiation center |
| 英文摘要 | Alkaline phytases from Bacillus species, which hydrolyze phytate to less phosphorylated myo-inositols and inorganic phosphate, have great potential as additives to animal feed. The thermostability and neutral optimum pH of Bacillus phytase are attributed largely to the presence of calcium ions. Nonetheless, no report has demonstrated directly how the metal ions coordinate phytase and its substrate to facilitate the catalytic reaction. In this study, the interactions between a phytate analog (myo-inositol hexasulfate) and divalent metal ions in Bacillus subtilis phytase were revealed by the crystal structure at 1.25 angstrom resolution. We found all, except the first, sulfates on the substrate analog have direct or indirect interactions with amino acid residues in the enzyme active site. The structures also unraveled two active site-associated metal ions that were not explored in earlier studies. Significantly, one metal ion could be crucial to substrate binding. In addition, binding of the fourth sulfate of the substrate analog to the active site appears to be stronger than that of the others. These results indicate that alkaline phytase starts by cleaving the fourth phosphate, instead of the third or the sixth that were proposed earlier. Our high-resolution, structural representation of Bacillus phytase in complex with a substrate analog and divalent metal ions provides new insight into the catalytic mechanism of alkaline phytases in general. (C) 2011 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | PURPLE ACID-PHOSPHATASE ; BETA-PROPELLER PHYTASE ; ACTIVE-SITE ; MECHANISM ; HYDROLYSIS ; PROGRAM ; ENZYME ; SUITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000291520100011 |
| 公开日期 | 2011-08-17 |
| 源URL | [http://localhost/handle/0/112]  |
| 专题 | 天津工业生物技术研究所_酶工程实验室 马延和 _期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China 2.Natl Taiwan Univ, Inst Biotechnol, Taipei 106, Taiwan 3.Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan 4.Natl Taiwan Univ, Inst Microbiol & Biochem, Taipei 106, Taiwan 5.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan 6.Acad Sinica, Inst Biomed Sci, Taipei 115, Taiwan 7.Acad Sinica, Agr Biotechnol Res Ctr, Taipei 115, Taiwan 8.Genozyme Biotechnol Inc, Taipei 106, Taiwan |
| 推荐引用方式 GB/T 7714 | Zeng, Yi-Fang,Ko, Tzu-Ping,Lai, Hui-Lin,et al. Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate[J]. JOURNAL OF MOLECULAR BIOLOGY,2011,409(2):214-224. |
| APA | Zeng, Yi-Fang.,Ko, Tzu-Ping.,Lai, Hui-Lin.,Cheng, Ya-Shan.,Wu, Tzu-Hui.,...&Liu, Je-Ruei.(2011).Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate.JOURNAL OF MOLECULAR BIOLOGY,409(2),214-224. |
| MLA | Zeng, Yi-Fang,et al."Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate".JOURNAL OF MOLECULAR BIOLOGY 409.2(2011):214-224. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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