Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars
文献类型：期刊论文
| 作者 | Chan, Hsiu-Chien1; Zhu, Yueming1; Hu, Yumei1; Ko, Tzu-Ping2; Huang, Chun-Hsiang1; Ren, Feifei1; Chen, Chun-Chi3; Ma, Yanhe1; Guo, Rey-Ting1; Sun, Yuanxia1 |
| 刊名 | PROTEIN & CELL
 |
| 出版日期 | 2012-02-01 |
| 卷号 | 3期号:2页码:123-131 |
| 关键词 | D-psicose 3-epimerase ketohexose complex structure |
| 英文摘要 | D-Psicose 3-epimerase (DPEase) is demonstrated to be useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature. Clostridium cellulolyticum H10 has recently been identified as a DPEase that can epimerize D-fructose to yield D-psicose with a much higher conversion rate when compared with the conventionally used DTEase. In this study, the crystal structure of the C. cellulolyticum DPEase was determined. The enzyme assembles into a tetramer and each subunit shows a (beta/alpha)8 TIM barrel fold with a Mn2+ metal ion in the active site. Additional crystal structures of the enzyme in complex with substrates/products (D-psicose, D-fructose, D-tagatose and D-sorbose) were also determined. From the complex structures of C. cellulolyticum DPEase with D-psicose and D-fructose, the enzyme has much more interactions with D-psicose than D-fructose by forming more hydrogen bonds between the substrate and the active site residues. Accordingly, based on these ketohexose-bound complex structures, a C3-O3 proton-exchange mechanism for the conversion between D-psicose and D-fructose is proposed here. These results provide a clear idea for the deprotonation/protonation roles of E150 and E244 in catalysis. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Cell Biology |
| 研究领域[WOS] | Cell Biology |
| 关键词[WOS] | D-TAGATOSE 3-EPIMERASE ; DIETARY D-PSICOSE ; D-FRUCTOSE ; AGROBACTERIUM-TUMEFACIENS ; ACTIVE-SITE ; RATS ; EPIMERIZATION ; BIOPRODUCTION ; SOFTWARE ; SUITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000310526200008 |
| 源URL | [http://124.16.173.210/handle/834782/1316]  |
| 专题 | 天津工业生物技术研究所_结构生物学与蛋白酶学实验室 郭瑞庭_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China 2.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan 3.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chan, Hsiu-Chien,Zhu, Yueming,Hu, Yumei,et al. Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars[J]. PROTEIN & CELL,2012,3(2):123-131. |
| APA | Chan, Hsiu-Chien.,Zhu, Yueming.,Hu, Yumei.,Ko, Tzu-Ping.,Huang, Chun-Hsiang.,...&Sun, Yuanxia.(2012).Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars.PROTEIN & CELL,3(2),123-131. |
| MLA | Chan, Hsiu-Chien,et al."Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars".PROTEIN & CELL 3.2(2012):123-131. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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