Knowledge Management System of Northwest Institute of Plateau Biology, CAS
| Computational studies on the catalytic mechanism of phosphoketolase | |
| Zhang, Jing1,2; Liu, Yongjun1,3; Liu, YJ (reprint author), Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China. | |
| 2013-12-01 | |
| 发表期刊 | COMPUTATIONAL AND THEORETICAL CHEMISTRY
 |
| ISSN | 2210-271X |
| 卷号 | 1025页码:1-7 |
| 文章类型 | Article |
| 摘要 | Phosphoketolase (PK) is a thiamine diphosphate (THDP) dependent enzyme which plays key roles in the metabolism of heterofermentative bacteria. By using density functional theory (DFT) method, the catalytic mechanism of PK has been studied on simplified models. The calculation results indicate hat the formation of 2-alpha,beta-dihydroxyethylidene-THDP (DHETHDP) and erythrose-4-phosphate (E4P) involves one C-C bond formation and one C-C bond cleavage process. Each C-C bond formation or cleavage is always accompanied by a proton transfer in a concerted but asynchronous way. The dehydration process in the reaction of PK is distinct from that of other THDP-dependent enzymes. The Keto-Enol tautomerism process is assisted with a mediator His553. His64, His553 and His97 are found to have the function to stabilize the transition states and intermediates. His64 is a better candidate of B1 catalyst. His553 acts as a proton donor to protonate the carbonyl oxygen, and plays intermediary role in the Keto-Enol tautomerism process. His97 is the probable B2 catalyst in the dehydration process. (C) 2013 Elsevier B.V. All rights reserved.; Phosphoketolase (PK) is a thiamine diphosphate (THDP) dependent enzyme which plays key roles in the metabolism of heterofermentative bacteria. By using density functional theory (DFT) method, the catalytic mechanism of PK has been studied on simplified models. The calculation results indicate hat the formation of 2-alpha,beta-dihydroxyethylidene-THDP (DHETHDP) and erythrose-4-phosphate (E4P) involves one C-C bond formation and one C-C bond cleavage process. Each C-C bond formation or cleavage is always accompanied by a proton transfer in a concerted but asynchronous way. The dehydration process in the reaction of PK is distinct from that of other THDP-dependent enzymes. The Keto-Enol tautomerism process is assisted with a mediator His553. His64, His553 and His97 are found to have the function to stabilize the transition states and intermediates. His64 is a better candidate of B1 catalyst. His553 acts as a proton donor to protonate the carbonyl oxygen, and plays intermediary role in the Keto-Enol tautomerism process. His97 is the probable B2 catalyst in the dehydration process. (C) 2013 Elsevier B.V. All rights reserved. |
| 关键词 | Phosphoketolase Density Functional Theory (Dft) Method Reaction Mechanism Thdp-dependent Enzyme Dehydration Keto-enol Tautomerism |
| WOS标题词 | Science & Technology ; Physical Sciences |
| 关键词[WOS] | DIPHOSPHATE-DEPENDENT ENZYMES ; THIAMIN DIPHOSPHATE ; PYRUVATE DECARBOXYLASE ; CRYSTAL-STRUCTURE ; LACTOBACILLUS-PLANTARUM ; ZYMOMONAS-MOBILIS ; TRANSKETOLASE ; ACTIVATION ; BIFIDOBACTERIUM ; BIOSYNTHESIS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS研究方向 | Chemistry |
| WOS类目 | Chemistry, Physical |
| WOS记录号 | WOS:000327806100001 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://210.75.249.4/handle/363003/3893 |
| 专题 | 中国科学院西北高原生物研究所 |
| 通讯作者 | Liu, YJ (reprint author), Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China. |
| 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,Liu, Yongjun,Liu, YJ . Computational studies on the catalytic mechanism of phosphoketolase[J]. COMPUTATIONAL AND THEORETICAL CHEMISTRY,2013,1025:1-7. |
| APA | Zhang, Jing,Liu, Yongjun,&Liu, YJ .(2013).Computational studies on the catalytic mechanism of phosphoketolase.COMPUTATIONAL AND THEORETICAL CHEMISTRY,1025,1-7. |
| MLA | Zhang, Jing,et al."Computational studies on the catalytic mechanism of phosphoketolase".COMPUTATIONAL AND THEORETICAL CHEMISTRY 1025(2013):1-7. |
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