Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase
文献类型：期刊论文
| 作者 | Yang, Yu1; Ko, Tzu-Ping2; Liu, Long1; Li, Jianghua1; Huang, Chun-Hsiang3; Chen, Jian1; Guo, Rey-Ting3; Du, Guocheng1 |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2014-09-26 |
| 卷号 | 452期号:3页码:509-514 |
| 关键词 | p-Nitrophenyl esters Lipase activity Enzyme kinetics Crystal structure Mutagenesis |
| 英文摘要 | Oxidized polyvinyl alcohol hydrolase (OPH) catalyzes the cleavage of C-C bond in beta-diketone. It belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site. The lid is the most variable region when pOPH from Pseudomonas sp. VM15C and sOPH from Sphingopyxis sp. 113P3 are compared. The wild-type enzymes and the pOPH mutants W255A, W255Y and W255F were analyzed for lipase activity by using p-nitrophenyl (pNP) esters as the substrates. The wild-type enzymes showed increased K-m and decreased k(cat)/K-m with the acyl chain length, and the mutants showed reduced k(cat)/K-m for pNP acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for pNP butyrate can be a result of product inhibition, as suggested by the complex crystal structures, in which butyric acid, DMSO or PEG occupied the same substrate-binding cleft. The mutant activity was retained with pNP caprylate and pNP laurate as the substrates, reflecting the amphipathic nature of the cleft. Moreover, the disulfide bond formation of Cys257/267 is important for the activity of pOPH, but it is not essential for sOPH, which has a shorter lid structure. (C) 2014 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | MALASSEZIA-GLOBOSA ; CRYSTAL-STRUCTURE ; FOLD ENZYMES ; LIPASE ; INSIGHTS ; SPECIFICITY ; DEGRADATION ; BINDING |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000343023900033 |
| 公开日期 | 2014-12-23 |
| 源URL | [http://124.16.173.210/handle/311007/533]  |
| 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.Jiangnan Univ, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Peoples R China 2.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Yu,Ko, Tzu-Ping,Liu, Long,et al. Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2014,452(3):509-514. |
| APA | Yang, Yu.,Ko, Tzu-Ping.,Liu, Long.,Li, Jianghua.,Huang, Chun-Hsiang.,...&Du, Guocheng.(2014).Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,452(3),509-514. |
| MLA | Yang, Yu,et al."Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 452.3(2014):509-514. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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