QM/MM study of the mechanism of enzymatic limonene 1,2-epoxide hydrolysis
文献类型：期刊论文
| 作者 | Hou, Q. Q.1; Sheng, X.1; Wang, J. H.1; Liu, Y. J.1,2; Liu, C. B.1 |
| 刊名 | biochimica et biophysica acta-proteins and proteomics
 |
| 出版日期 | 2012-02-01 |
| 卷号 | 1824期号:2页码:263-268 |
| 关键词 | QM/MM Hydrolases Epoxide ring-opening Reaction mechanism Mutation |
| ISSN号 | 1570-9639 |
| 中文摘要 | limonene 1,2-epoxide hydrolase (leh) is completely different from those of classic epoxide hydrolases (ehs) which catalyze the hydrolysis of epoxides to vicinal diols. a novel concerted general acid catalysis step involving the asp101-arg99-asp132 triad is proposed to play an important role in the mechanism. combined quantum-mechanical/molecular-mechanical (qm/mm) calculations gave activation barriers of 16.9 and 25.1 kcal/mol at the b3lyp/6-31g(d,p)//charmm level for nucleophilic attack on the more and less substituted epoxide carbons, respectively. furthermore, the important roles of residues arg99, tyr53 and asn55 on mutated leh were evaluated by qm/mm-scanned energy mapping. these results may provide an explanation for site-directed mutagenesis. (c) 2011 elsevier b.v. all rights reserved. |
| 英文摘要 | limonene 1,2-epoxide hydrolase (leh) is completely different from those of classic epoxide hydrolases (ehs) which catalyze the hydrolysis of epoxides to vicinal diols. a novel concerted general acid catalysis step involving the asp101-arg99-asp132 triad is proposed to play an important role in the mechanism. combined quantum-mechanical/molecular-mechanical (qm/mm) calculations gave activation barriers of 16.9 and 25.1 kcal/mol at the b3lyp/6-31g(d,p)//charmm level for nucleophilic attack on the more and less substituted epoxide carbons, respectively. furthermore, the important roles of residues arg99, tyr53 and asn55 on mutated leh were evaluated by qm/mm-scanned energy mapping. these results may provide an explanation for site-directed mutagenesis. (c) 2011 elsevier b.v. 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] | agrobacterium-radiobacter ad1 ; epoxide hydrolase ; catalytic mechanism ; molecular-dynamics ; limonene-1,2-epoxide hydrolase ; active-site ; intermediate ; tyrosine ; program ; models |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000299986300001 |
| 公开日期 | 2013-03-15 |
| 源URL | [http://ir.nwipb.ac.cn/handle/363003/3724]  |
| 专题 | 西北高原生物研究所_中国科学院西北高原生物研究所 |
| 作者单位 | 1.Shandong Univ, Key Lab Colloid & Interface Chem, Minist Educ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China 2.Chinese Acad Sci, Key Lab Adaptat & Evolut Plateau Biota, NW Inst Plateau Biol, Xining 810008, Qinghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Hou, Q. Q.,Sheng, X.,Wang, J. H.,et al. QM/MM study of the mechanism of enzymatic limonene 1,2-epoxide hydrolysis[J]. biochimica et biophysica acta-proteins and proteomics,2012,1824(2):263-268. |
| APA | Hou, Q. Q.,Sheng, X.,Wang, J. H.,Liu, Y. J.,&Liu, C. B..(2012).QM/MM study of the mechanism of enzymatic limonene 1,2-epoxide hydrolysis.biochimica et biophysica acta-proteins and proteomics,1824(2),263-268. |
| MLA | Hou, Q. Q.,et al."QM/MM study of the mechanism of enzymatic limonene 1,2-epoxide hydrolysis".biochimica et biophysica acta-proteins and proteomics 1824.2(2012):263-268. |
入库方式： OAI收割
来源：西北高原生物研究所
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