Biochemical basis for hydrolysis of organophosphorus by a marine bacterial prolidase
文献类型：期刊论文
| 作者 | Xiao, YZ; Yang, J; Tian, XP; Wang, XX; Li, J; Zhang, S; Long, LJ |
| 刊名 | PROCESS BIOCHEMISTRY
 |
| 出版日期 | 2017 |
| 卷号 | 52页码:141-148 |
| 关键词 | Enzyme promiscuity Organophosphorus bioremediation Organophosphorus acid anhydrolase Prolidase |
| 通讯作者 | yangjian@scsio.ac.cn ; longlj@scsio.ac.cn |
| 中文摘要 | Extensive application of synthesized organophosphorus compounds (OPs) leads to pollutant accumulation and enhanced eco-toxicity. Hydrolysis of phosphotriester bonds catalyzed by evolved microbial enzymes is a key step for detoxification of OPs. Here, a new marine bacterial prolidase OPAA4301 exhibiting promiscuous phosphotriesterase activity was isolated and systematically characterized. The homo-tetrameric enzyme OPAA4301 can catalyze the hydrolysis of both amido bond and phosphotriester bond. Manganese ions were observed to be essential for its catalytic integrity, and in vitro substitution of manganese ions by different metal cofactors led to decreased activity. We also revealed cooperation pattern of metal ligands and substrate-binding residues on OP hydrolysis by mutational analysis. Metal-binding sites together with Arg418 in the large-binding pocket of the enzyme were found to be indispensable for catalytic ability. Substitution mutation of small- and large-binding pocket residues caused significant variation in phosphotriesterase activity, and leaving group sites appeared to be involved in the catalytic process as substrate affinity regulators. Our study gave an overall biochemical understanding on the organophosphorus hydrolysis pattern of the newly identified marine bacterial prolidase and provided ideas for protein engineering to expand its application in the bioremediation field. (C) 2016 Elsevier Ltd. All rights reserved. |
| 源URL | [http://ir.scsio.ac.cn/handle/344004/16216]  |
| 专题 | 南海海洋研究所_中科院海洋生物资源可持续利用重点实验室 |
| 推荐引用方式 GB/T 7714 | Xiao, YZ,Yang, J,Tian, XP,et al. Biochemical basis for hydrolysis of organophosphorus by a marine bacterial prolidase[J]. PROCESS BIOCHEMISTRY,2017,52:141-148. |
| APA | Xiao, YZ.,Yang, J.,Tian, XP.,Wang, XX.,Li, J.,...&Long, LJ.(2017).Biochemical basis for hydrolysis of organophosphorus by a marine bacterial prolidase.PROCESS BIOCHEMISTRY,52,141-148. |
| MLA | Xiao, YZ,et al."Biochemical basis for hydrolysis of organophosphorus by a marine bacterial prolidase".PROCESS BIOCHEMISTRY 52(2017):141-148. |
入库方式： OAI收割
来源：南海海洋研究所
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