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The difference in the carboxy-terminal sequence is responsible for the difference in the activity of chicken and rat liver fructose-2,6-bisphosphatase
文献类型：期刊论文
| 作者 | Zhu, Z; Ling, S; Yang, QH; Li, L |
| 刊名 | BIOLOGICAL CHEMISTRY
 |
| 出版日期 | 2000 |
| 卷号 | 381期号:12页码:1195-1202 |
| 关键词 | 6-phosphofructo-2-kinase fructose-2 kinetic property mutagenesis separate domain 6-bisphosphatase |
| 通讯作者 | Li, L (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China., |
| 英文摘要 | The fructose-2,6-bisphosphatase domain of the bifunctional chicken liver enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase shares approximately 95% amino acid sequence homology with that of the rat enzyme. However, these two enzymes are significantly different in their phosphatase activities. In this report, we show that the COOH-terminal 25 amino acids of the two enzymes are responsible for the different enzymatic activities. Although these 25 amino acids are not required for the phosphatase activity, their removal diminishes the differences in the activities between the two enzymes. In addition, two chimeric molecules (one consisting of the catalytic core of the chicken bisphosphatase domain and the rat COOH-terminal 25 amino acids, and the other consisting of most of the intact chicken enzyme and the rat COOH-terminal 25 amino acids) showed the same kinetic properties as the rat enzyme. Furthermore, substitution of the residues Pro(456)Pro(457)Ala(458) Of th, chicken enzyme with GluAlaGlu, the corresponding sequence in the rat liver enzyme, yields a chicken enzyme that behaves like the rat enzyme. These results demonstrate that the different bisphosphatase activities of the chicken and rat liver bifunctional enzymes can be attributed to the differences in their COOH-terminal amino acid sequences, particularly the three residues. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | AMINO-ACID-SEQUENCE ; 6-PHOSPHOFRUCTO-2-KINASE FRUCTOSE-2,6-BISPHOSPHATASE ; BIFUNCTIONAL ENZYME ; MOLECULAR-CLONING ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; PROTEIN-KINASE ; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE ; EXPRESSION ; 2,6-BISPHOSPHATASE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000166643600006 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2745]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Zhu, Z,Ling, S,Yang, QH,et al. The difference in the carboxy-terminal sequence is responsible for the difference in the activity of chicken and rat liver fructose-2,6-bisphosphatase[J]. BIOLOGICAL CHEMISTRY,2000,381(12):1195-1202. |
| APA | Zhu, Z,Ling, S,Yang, QH,&Li, L.(2000).The difference in the carboxy-terminal sequence is responsible for the difference in the activity of chicken and rat liver fructose-2,6-bisphosphatase.BIOLOGICAL CHEMISTRY,381(12),1195-1202. |
| MLA | Zhu, Z,et al."The difference in the carboxy-terminal sequence is responsible for the difference in the activity of chicken and rat liver fructose-2,6-bisphosphatase".BIOLOGICAL CHEMISTRY 381.12(2000):1195-1202. |
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