Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation
文献类型：期刊论文
| 作者 | Bai, Wenqin1,2,3; Zhou, Cheng2; Zhao, Yueju4; Wang, Qinhong1; Ma, Yanhe1,2 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2015-07-10 |
| 卷号 | 10期号:7 |
| 英文摘要 | To understand the molecular basis of higher pH catalytic adaptation of family 11 xylanases, we compared the structures of alkaline, neutral, and acidic active xylanases and analyzed mutants of xylanase Xyn11A-LC from alkalophilic Bacillus sp. SN5. It was revealed that alkaline active xylanases have increased charged residue content, an increased ratio of negatively to positively charged residues, and decreased Ser, Thr, and Tyr residue content relative to non-alkaline active counterparts. Between strands beta 6 and beta 7, alkaline xylanases substitute an alpha-helix for a coil or turn found in their non-alkaline counterparts. Compared with non-alkaline xylanases, alkaline active enzymes have an inserted stretch of seven amino acids rich in charged residues, which may be beneficial for xylanase function in alkaline conditions. Positively charged residues on the molecular surface and ionic bonds may play important roles in higher pH catalytic adaptation of family 11 xylanases. By structure comparison, sequence alignment and mutational analysis, six amino acids (Glu16, Trp18, Asn44, Leu46, Arg48, and Ser187, numbering based on Xyn11A-LC) adjacent to the acid/base catalyst were found to be responsible for xylanase function in higher pH conditions. Our results will contribute to understanding the molecular mechanisms of higher pH catalytic adaptation in family 11 xylanases and engineering xylanases to suit industrial applications. |
| WOS标题词 | Science & Technology |
| 类目[WOS] | Multidisciplinary Sciences |
| 研究领域[WOS] | Science & Technology - Other Topics |
| 关键词[WOS] | BACILLUS SP SN5 ; TRICHODERMA-REESEI ; 3-DIMENSIONAL STRUCTURE ; ALKALINE ADAPTATION ; THERMAL-STABILITY ; CRYSTAL-STRUCTURE ; ENZYME ; GLYCOSIDASE ; EXPRESSION ; INCREASES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000358162300179 |
| 源URL | [http://124.16.173.210/handle/834782/1504]  |
| 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, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China 2.Chinese Acad Sci, Inst Microbiol, Natl Engn Lab Ind Enzymes, Beijing 100101, Peoples R China 3.Shanxi Normal Univ, Sch Life Sci, Linfen 041004, Peoples R China 4.Chinese Acad Agr Sci, Inst Agroprod Proc Sci & Technol, Beijing 100193, Peoples R China |
| 推荐引用方式 GB/T 7714 | Bai, Wenqin,Zhou, Cheng,Zhao, Yueju,et al. Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation[J]. PLOS ONE,2015,10(7). |
| APA | Bai, Wenqin,Zhou, Cheng,Zhao, Yueju,Wang, Qinhong,&Ma, Yanhe.(2015).Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation.PLOS ONE,10(7). |
| MLA | Bai, Wenqin,et al."Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation".PLOS ONE 10.7(2015). |
入库方式： OAI收割
来源：天津工业生物技术研究所
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