Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sucrose non-fermenting-1-related protein kinase 1 (SnRK1) has been shown to play an essential role in regulating saccharide metabolism and starch biosynthesis of plant. The regulatory role of StSnRK1 from potato in regulating carbohydrate metabolism and starch accumulation has not been investigated. In this work, a cDNA encoding the SnRK1 protein, named StSnRK1, was isolated from potato. The open reading frame contained 1545 nucleotides encoding 514 amino acids. Subcellular localization analysis in onion epidermal cells indicated that StSnRK1 protein was localized to the nucleus. The coding region of StSnRK1 was cloned into a binary vector under the control of 35S promoter and then transformed into tobacco to obtain transgenic plants. Transgenic tobacco plants expressing StSnRK1 were shown to have a significant increased accumulation of starch content, as well as sucrose, glucose and fructose content. Real-time quantitative PCR analysis indicated that overexpression of StSnRK1 up-regulated the expression of sucrose synthase (NtSUS), ADP-glucose pyrophosphorylase (NtAGPase) and soluble starch synthase (NtSSS III) genes involved in starch biosynthesis in the transgenic plants. In contrast, the expression of sucrose phosphate synthase (NtSPS) gene was decreased in the transgenic plants. Meanwhile, enzymatic analyses indicated that the activities of major enzymes (SUS, AGPase and SSS) involved in the starch biosynthesis were enhanced, whereas SPS activity was decreased in the transgenic plants compared to the wild-type. These results suggest that the manipulation of StSnRK1 expression might be used for improving quality of plants in the future.
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PMID:A sucrose non-fermenting-1-related protein kinase 1 gene from potato, StSnRK1, regulates carbohydrate metabolism in transgenic tobacco. 2915 40

Sucrose is utilized as an initial material for production of the storage substances. Sucrose synthase reversibly catalyzes reactions of the sucrose degradation and its synthesis between sucrose with UDP and UDP-glucose with fructose. They also had the activity of the reactions for sucrose degradation of sucrose with ADP, and sucrose synthesis from ADP-glucose and fructose. Rice has three representative isoforms of sucrose synthase, Rsus1, Rsus2, and Rsus3, in which Rsus1 and Rsus3 are highly expressed in developing seeds. These three isoforms were phosphorylated by SPK, a calcium-dependent protein kinase. By phosphorylation, they showed increase of their reactivity for sucrose degradation on both reactions using UDP and ADP. In contrast, the synthetic activity of these isoforms was not altered by phosphorylation in any cases of the reactions with UDP-glucose and ADP-glucose. These results indicated that phosphorylation of sucrose synthase isoforms selectively led to enhance the reactivity for sucrose degradation.
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PMID:Phosphorylation of rice sucrose synthase isoforms promotes the activity of sucrose degradation. 3127 15

Free (soluble, non-protein) asparagine concentration can increase many-fold in wheat grain in response to sulphur deficiency. This exacerbates a major food safety and regulatory compliance problem for the food industry because free asparagine may be converted to the carcinogenic contaminant, acrylamide, during baking and processing. Here, we describe the predominant route for the conversion of asparagine to acrylamide in the Maillard reaction. The effect of sulphur deficiency and its interaction with nitrogen availability is reviewed, and we reiterate our advice that sulphur should be applied to wheat being grown for human consumption at a rate of 20 kg per hectare. We describe the genetic control of free asparagine accumulation, including genes that encode metabolic enzymes (asparagine synthetase, glutamine synthetase, glutamate synthetase, and asparaginase), regulatory protein kinases (sucrose nonfermenting-1 (SNF1)-related protein kinase-1 (SnRK1) and general control nonderepressible-2 (GCN2)), and basic leucine zipper (bZIP) transcription factors, and how this genetic control responds to sulphur, highlighting the importance of asparagine synthetase-2 (ASN2) expression in the embryo. We show that expression of glutamate-cysteine ligase is reduced in response to sulphur deficiency, probably compromising glutathione synthesis. Finally, we describe unexpected effects of sulphur deficiency on carbon metabolism in the endosperm, with large increases in expression of sucrose synthase-2 (SuSy2) and starch synthases.
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PMID:The Sulphur Response in Wheat Grain and Its Implications for Acrylamide Formation and Food Safety. 3248 24

Sucrose controls various developmental and metabolic processes in plants. In this review, we evaluate whether sucrose could be a preferred signaling molecule that controls processes like carbohydrate metabolism, accumulation of storage proteins, sucrose transport, anthocyanin accumulation, and floral induction. We summarize putative sucrose-dependent signaling pathways. Sucrose, but not other sugars, stimulates the genes that encode ADP-glucose pyrophosphorylase (AGPase), granule-bound starch synthase I, and UDP-glucose pyrophosphorylase in several species. The class-1 patatin promoter is induced under high sucrose conditions in potato (Solanum tuberosum). Exogenous sucrose reduces the loading of sucrose to the phloem by inhibiting the expression of the sucrose transporter and its protein activity in sugar beet (Beta vulgaris). Sucrose also influences a wide range of growth processes, including cell division, ribosome synthesis, cotyledon development, far-red light signaling, and tuber development. Floral induction is promoted by sucrose in several species. The molecular mechanisms by which sucrose functions as a signal are largely unknown. Sucrose enhances the expression of transcription factors such as AtWRKY20 and MYB75, which function upstream of the sucrose-responsive genes. Sucrose controls the expression of AtbZIP11 at the post-transcriptional level by the peptide encoded by uORF2. Sucrose levels affect translation of a group of mRNAs in Arabidopsis. Sucrose increases the activity of AGPase by posttranslational redox-modification. Sucrose interrupts the interaction between sucrose transporter SUT4 and cytochrome b5. In addition, the SNF-related protein kinase-1 appears to be involved in sucrose-dependent pathways by controlling sucrose synthase (SUS4) expression.
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PMID:Sucrose signaling in higher plants. 3328 16


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