Knowledge Management System of Northwest Institute of Plateau Biology, CAS
| Theoretical Investigation on the Dissociation of (R)-Benzoin Catalyzed by Benzaldehyde Lyase | |
| Zhang, Jing1,2; Sheng, Xiang3; Hou, QianQian3; Liu, Yongjun1,3 | |
| 2014-03-15 | |
| 发表期刊 | INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY
 |
| ISSN | 0020-7608 |
| 卷号 | 114期号:6页码:375-382 |
| 文章类型 | Article |
| 摘要 | Benzaldehyde lyase (BAL) is a versatile thiamin diphosphate (THDP)-dependent enzyme with widespread synthetic applications in industry. Besides lyase activity, BAL also performs the functions as carboligase and decarboxylase. Unlike many other THDP-dependent enzymes, the active center of BAL is devoid of any acid-base amino acid residues except Glu50 and His29, and therefore, the catalytic mechanism of BAL is unusual. In this article, the dissociation mechanism of (R)-benzoin to benzaldehyde catalyzed by BAL has been studied by using density functional theory method. The calculation results indicate that the whole reaction consists of four elementary steps, and at least two steps contribute to rate-limiting. A big difference with other THDP-dependent enzymes is that, in the first stage of the reaction, the ligation of substrate and THDP ylide is not companied by proton transfer, and in the subsequent transition states and intermediates, the carbonyl oxygen always exists in the form of anion. Gln113, His29, and 4-amino group of THDP are found to have the function to stabilize the transition states and intermediates. His29 acts as the proton acceptor in step 2 and proton donor in step 3 using one water molecule as mediator. (c) 2013 Wiley Periodicals, Inc.; Benzaldehyde lyase (BAL) is a versatile thiamin diphosphate (THDP)-dependent enzyme with widespread synthetic applications in industry. Besides lyase activity, BAL also performs the functions as carboligase and decarboxylase. Unlike many other THDP-dependent enzymes, the active center of BAL is devoid of any acid-base amino acid residues except Glu50 and His29, and therefore, the catalytic mechanism of BAL is unusual. In this article, the dissociation mechanism of (R)-benzoin to benzaldehyde catalyzed by BAL has been studied by using density functional theory method. The calculation results indicate that the whole reaction consists of four elementary steps, and at least two steps contribute to rate-limiting. A big difference with other THDP-dependent enzymes is that, in the first stage of the reaction, the ligation of substrate and THDP ylide is not companied by proton transfer, and in the subsequent transition states and intermediates, the carbonyl oxygen always exists in the form of anion. Gln113, His29, and 4-amino group of THDP are found to have the function to stabilize the transition states and intermediates. His29 acts as the proton acceptor in step 2 and proton donor in step 3 using one water molecule as mediator. (c) 2013 Wiley Periodicals, Inc. |
| 关键词 | Benzaldehyde Lyase Density Functional Theory Method Reaction Mechanism Thdp-dependent Enzyme R-benzoin |
| WOS标题词 | Science & Technology ; Physical Sciences |
| 关键词[WOS] | DIPHOSPHATE-DEPENDENT ENZYMES ; ALPHA-HYDROXY KETONES ; THIAMIN DIPHOSPHATE ; PYRUVATE DECARBOXYLASE ; BENZOYLFORMATE DECARBOXYLASE ; PSEUDOMONAS-FLUORESCENS ; ANGSTROM RESOLUTION ; CRYSTAL-STRUCTURE ; MECHANISM ; ACTIVATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS研究方向 | Chemistry ; Mathematics ; Physics |
| WOS类目 | Chemistry, Physical ; Mathematics, Interdisciplinary Applications ; Physics, Atomic, Molecular & Chemical |
| WOS记录号 | WOS:000330577400002 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://210.75.249.4/handle/363003/4245 |
| 专题 | 中国科学院西北高原生物研究所 |
| 作者单位 | 1.Chinese Acad Sci, Northwest Inst Plateau Biol, Xining 810001, Qinghai, Peoples R China 2.Jining Univ, Key Lab Inorgan Chem Univ Shandong, Qufu 273155, Shandong, Peoples R China 3.Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Jing,Sheng, Xiang,Hou, QianQian,et al. Theoretical Investigation on the Dissociation of (R)-Benzoin Catalyzed by Benzaldehyde Lyase[J]. INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,2014,114(6):375-382. |
| APA | Zhang, Jing,Sheng, Xiang,Hou, QianQian,&Liu, Yongjun.(2014).Theoretical Investigation on the Dissociation of (R)-Benzoin Catalyzed by Benzaldehyde Lyase.INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,114(6),375-382. |
| MLA | Zhang, Jing,et al."Theoretical Investigation on the Dissociation of (R)-Benzoin Catalyzed by Benzaldehyde Lyase".INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY 114.6(2014):375-382. |
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