中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
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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.

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来源:西北高原生物研究所

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