Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa
文献类型：期刊论文
| 作者 | Feng XM1; Yang CL2; Zheng WY3; Wen JF[*]2 |
| 刊名 | CHINESE MEDICAL JOURNAL
 |
| 出版日期 | 2014 |
| 卷号 | 127期号:23页码:4097-4103 |
| 关键词 | pyruvate phosphate dikinase (PPDK) Giardia lamblia adaptive evolution Amitochondriate protozoa 3-dimensional (3-D) structures |
| 通讯作者 | wenjf@mail.kiz.ac.cn |
| 合作状况 | 其它 |
| 英文摘要 | Background Pyruvate phosphate dikinase (PPDK) reversibly catalyzes the interconversion of phosphoenolpyruvate (PEP) and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. Molecular modeling of PPDKs from divergent organisms demonstrates that the orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis. The goal of this study was to determine whether PDDK from Giardia underwent adaptive evolution in order to produce more energy under anaerobic conditions. Methods A total of 123 PPDK sequences from protozoans, proteobacteria, plants, and algae were selected, based upon sequence similarities to Giardia lamblia PPDK and Zea mays PPDK. Three-dimensional (3-D) models were generated for PPDKs from divergent organisms and were used to compare the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs were compared using a maximum-likelihood tree. Results For PPDK from Giardia, as well as from other anaerobic protozoans, the central domain tilted toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzed ATP synthesis. Furthermore, the orientation of this central domain was determined by interactions between the N- and C-terminal domains. Phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species suggested that PPDK has likely undergone adaptive evolution in response to differences in environmental and metabolic conditions. Conclusion These results suggested that PPDK in anaerobic organisms is functionally adapted to generate energy more efficiently in an anaerobic environment. |
| 收录类别 | SCI |
| 资助信息 | This work was supported by grants from the State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences (No. GREKF08-07), the National Natural Science Foundation of China (No. 81301450) and the Jilin Provincial Science and Technology Department of China (No. 20130413035GH) |
| 语种 | 英语 |
| WOS记录号 | WOS:000347276500018 |
| 公开日期 | 2015-02-03 |
| 源URL | [http://159.226.149.42:8088/handle/152453/8245]  |
| 专题 | 昆明动物研究所_真核细胞进化基因组 昆明动物研究所_遗传资源与进化国家重点实验室 |
| 作者单位 | 1.The School of Laboratory Medicine, Jilin Medical College, Jilin, Jilin 132013, China 2.State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China 3.The Department of Hand Microsurgery, Central Hospital of Jilin City, Jilin, Jilin 132000, China |
| 推荐引用方式 GB/T 7714 | Feng XM,Yang CL,Zheng WY,et al. Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa[J]. CHINESE MEDICAL JOURNAL,2014,127(23):4097-4103. |
| APA | Feng XM,Yang CL,Zheng WY,&Wen JF[*].(2014).Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa.CHINESE MEDICAL JOURNAL,127(23),4097-4103. |
| MLA | Feng XM,et al."Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa".CHINESE MEDICAL JOURNAL 127.23(2014):4097-4103. |
入库方式： OAI收割
来源：昆明动物研究所
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