Kinetics and docking studies on the effect of chemical modification of NADH for redox reactions with dehydrogenases
文献类型：期刊论文
| 作者 | Ma, Hongjing1,3; Zhang, Songping1; Su, Zhiguo1; Wang, Ping2 |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2012-05-01 |
| 卷号 | 77期号:0页码:111-118 |
| 关键词 | 8-(6-Aminohexyl)-amino-NADH Molecular docking Alcohol dehydrogenase Lactate dehydrogenase |
| ISSN号 | 1381-1177 |
| 通讯作者 | Zhang, SP |
| 英文摘要 | Cofactor analogs promise important applications in biosynthesis. The effect of chemical modification on the reactivity of NADH for redox reactions catalyzed by dehydrogenases was examined in this work. Compared with the native NADH, kinetics and molecular docking studies with 8-(6-aminohexyl)-amino-NADH showed that its binding with alcohol dehydrogenase (ADH) was not much affected or even enhanced by a factor of 4.9-fold with lactate dehydrogenase (LDH), but complicated the binding of substrates to the enzymes. For ADH, the Michaelis constant for acetaldehyde decreased from 0.47 to 0.048 mM, while that of sodium pyruvate with LDH increased to 0.81 from 0.18 mM. On the other hand, the modified coenzyme showed a 19.3-fold decrease in turnover number (k(cat)) with ADH, while a slight increase with LDH. Molecular docking analysis showed that the hexanediamine arm on the modified coenzyme generated an extra hydrogen bond at the active site of ADH, as well as additional hydrophobic interactions with both ADH and LDH. It appeared that the apparently decreased reactivity of modified cofactor with ADH was caused mainly by the enhanced stability of ternary coenzyme-enzyme-substrate complex, while in the case of LDH, the reduced substrate binding as a result of the chemical modification of NADH led to a slight increase in the overall reaction reactivity. (C) 2012 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | YEAST ALCOHOL-DEHYDROGENASE ; D-LACTATE DEHYDROGENASE ; LOCKING-ON STRATEGY ; HORSE LIVER ; SUBSTRATE-SPECIFICITY ; MOLECULAR MECHANICS ; BIOAFFINITY PURIFICATION ; AFFINITY CHROMATOGRAPHY ; COFACTOR REGENERATION ; COENZYME SPECIFICITY |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000302106400017 |
| 公开日期 | 2013-10-23 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/3870]  |
| 专题 | 过程工程研究所_生化工程国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 2.Univ Minnesota, Inst Biotechnol, Dept Bioprod & Biosyst Engn, St Paul, MN 55108 USA 3.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ma, Hongjing,Zhang, Songping,Su, Zhiguo,et al. Kinetics and docking studies on the effect of chemical modification of NADH for redox reactions with dehydrogenases[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2012,77(0):111-118. |
| APA | Ma, Hongjing,Zhang, Songping,Su, Zhiguo,&Wang, Ping.(2012).Kinetics and docking studies on the effect of chemical modification of NADH for redox reactions with dehydrogenases.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,77(0),111-118. |
| MLA | Ma, Hongjing,et al."Kinetics and docking studies on the effect of chemical modification of NADH for redox reactions with dehydrogenases".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 77.0(2012):111-118. |
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来源：过程工程研究所
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