Regulation of Sucrose Metabolism in Higher Plants: Localization and regulation of Activity of Key Enzymes

2000 ◽  
Vol 19 (1) ◽  
pp. 31-67 ◽  
Author(s):  
H. Winter ◽  
S. C. Huber
Sugar Tech ◽  
2013 ◽  
Vol 15 (2) ◽  
pp. 177-186 ◽  
Author(s):  
Ai-Qin Wang ◽  
Wen-Jing Huang ◽  
Jun-Qi Niu ◽  
Ming Liu ◽  
Li-Tao Yang ◽  
...  

2015 ◽  
Vol 35 (3) ◽  
Author(s):  
Muqing Zhang ◽  
Xiaolei Zhuo ◽  
Jihua Wang ◽  
Chuanyu Yang ◽  
Charles A. Powell ◽  
...  

2020 ◽  
Vol 7 (1) ◽  
Author(s):  
Xingxing Wang ◽  
Yi Chen ◽  
Shu Jiang ◽  
Feng Xu ◽  
Hongfei Wang ◽  
...  

Abstract Sucrose metabolism, particularly the decomposition of sucrose by invertase, plays a central role in plant responses to cold stress. Invertase inhibitors (INHs) evolved in higher plants as essential regulators of sucrose metabolism. By limiting invertase activity, INHs keep cellular sugar levels elevated, which provides enhanced protection to plants under stress. Our results showed that the expression of PpVIN2, the only vacuolar invertase (VIN) gene in peach fruit sensitive to chilling temperatures, increases significantly during cold storage, while VIN enzyme activity increases more modestly. We also found that peach fruit transiently overexpressing PpINH1 had decreased VIN activity. Interactions of PpINH1 and PpVIN2 with recombinant proteins were shown by yeast two-hybrid assays and bimolecular fluorescence complementation assays, as well as in vitro. During cold storage, trehalose-treated peach fruit had significantly increased PpINH1 expression, decreased VIN enzyme activity, and significantly higher sucrose content than did untreated fruit. As a result, the treated fruit had enhanced resistance to chilling injury. Collectively, our data show that the post-translational repression of VIN enzyme activity by PpINH1 helps maintain sucrose levels in peach fruit during cold storage, thereby improving resistance to chilling injury.


2010 ◽  
Vol 5 (7) ◽  
pp. 1934578X1000500 ◽  
Author(s):  
Chang Ling Zhao ◽  
Xiu Ming Cui ◽  
Yan Ping Chen ◽  
Quan Liang

Triterpenoid saponins are one of the key active components of many medicinal plants. The biosynthetic pathway of triterpenoid saponins in higher plants and a lot of experimental results both indicated that the key enzymes involved in triterpenoid saponin synthesis are squalene synthase (SS), squalene epoxidase (SE), lupeol synthase (LS), dammarenediol synthase (DS), β-amyrin synthase (β-AS), cytochrome P450-dependent monooxygenase (PDMO), and glycosyltransferase (GT). The activities and coding genes of the key enzymes could be induced by a range of factors in various plant species. However, the effects of the factors on the content and composition of the triterpenoid saponins in specific plants are not certainly coincident, and different factors appear to induce the gene expressions of the key enzymes by different signal pathways and at different levels. This paper could provide a reference for strengthening the triterpenoid saponin-synthesizing capability of specific medicinal plants at enzyme and/or gene expression levels in order to improve the plants’ commercial values.


1966 ◽  
Vol 100 (3) ◽  
pp. 577-588 ◽  
Author(s):  
J Ingle ◽  
K W Joy ◽  
R H Hageman

1. Possible mechanisms regulating the activities of three enzymes involved in nitrate assimilation, nitrate reductase, nitrite reductase and glutamate dehydrogenase, were studied in radish cotyledons. 2. Nitrate-reductase and nitrite-reductase activities are low in nitrogen-deficient cotyledons, and are induced by their substrates. 3. Glutamate dehydrogenase is present regardless of the nitrogen status, and the enzyme can be increased only slightly by long-term growth on ammonia. 4. Although nitrate is the best inducer of nitrate reductase, lower levels of induction are also obtained with nitrite and ammonia. The experiments did not distinguish between direct or indirect induction by these two molecules. 5. Nitrite reductase is induced by nitrite and only indirectly by nitrate. 6. The induction of both nitrate reductase and nitrite reductase is prevented by the inhibitors actinomycin D, puromycin and cycloheximide, indicating a requirement for the synthesis of RNA and protein. 7. The decay of nitrate reductase, determined after inhibition of protein synthesis, is slower than the synthesis of the enzyme. Nitrite reductase is much more stable than nitrate reductase. 8. The synthesis of nitrate reductase is not repressed by ammonia, but is repressed by growth on a nitrite medium. 9. There is no inhibition of nitrate reductase, nitrite reductase or glutamate dehydrogenase by the normal end products of assimilation, but cyanate is a fairly specific inhibitor of nitrate reductase.


Sign in / Sign up

Export Citation Format

Share Document