Distinct properties of two glutamine synthetase isoforms in soybean root nodules
| Autor: | Y. S. Tian, R. T. Wang, W. Zhao, J. X, X. J. Xing, X. Y. Fu, R. H. Peng, Q. H. Yao |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Gene isoform Root nodule Gs alpha subunit Biology 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Isozyme 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Glutamine synthetase Nitrogen fixation Transferase Ammonium 010606 plant biology & botany |
| Zdroj: | Applied Biochemistry and Microbiology. 52:643-649 |
| ISSN: | 1608-3024 0003-6838 |
| DOI: | 10.1134/s0003683816060156 |
| Popis: | Glutamine synthetase (GS) in nodule cytosol plays a major role in the assimilation of the ammonium produced by biological nitrogen fixation. To characterize the GS protein family in Glycine max root nodules, the catalytical properties of 2 GS1 isoenzymes (GS1β1 and GS1γ1) were compared in this study. Although, GmGS1β1 and GmGS1γ1 have very similar kinetic characteristics, they also exhibit distinct enzymatic properties in terms of thermal stability and the transferase to synthetase activity (GSt/GSs) ratios. The results demonstrated that GmGS1γ1, which displayed lower thermal stability and GSt/GSs ratios than GmGS1β1, might be considered as superior isoform to participate in the efficient assimilation of ammonia only when it is needed. Also, it is proposed that the difference of enzymatic properties between isoforms contribute to their differential roles in ammonia assimilation under variable internal and external environments. |
| Databáze: | OpenAIRE |
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