Topic
Pyruvate kinase
About: Pyruvate kinase is a research topic. Over the lifetime, 5683 publications have been published within this topic receiving 180020 citations. The topic is also known as: ATP:pyruvate 2-O-phosphotransferase & phosphoenolpyruvate kinase.
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TL;DR: The biosynthesis of the four proteins is sensitive to the nature of the carbon sources as well as to the shift from aerobic to anaerobic conditions.
97 citations
TL;DR: The presence of this transcription factor in rat islets and INS-1 cells is reported and unprecedented results suggest that ChREBP rather than USF mediates glucose-promoted L-PK expression in insulin-secreting cells.
97 citations
TL;DR: Light is shed on the potential role of protein phosphorylation on regulating meat quality development by analyzing the proteinosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24 h.
Abstract: Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24 h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1 h, but lowest at 24 h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p<0.05). Protein identification revealed that most of the phosphoproteins were glycometabolism-related enzymes, and the others were involved in stress response, phosphocreatine metabolism, and other functions. The phosphorylation of pyruvate kinase and triosephosphate isomerase-1 showed to be related to PM muscle pH decline rate. Our work sheds light on the potential role of protein phosphorylation on regulating meat quality development.
97 citations
TL;DR: Since previous studies demonstrated an increase in steady state glyceraldehyde-3-phosphate dehydrogenase RNA during low Oz exposure it is concluded that the level of this RNA is regulated post transcriptionally whereas the other four glycolytic enzyme RNAs are regulated at least partially at thelevel of transcription by oxygen availability.
Abstract: Cytoplasmic β-actin and five glycolytic enzyme cDNAs were isolated from a rat skeletal muscle cDNA library and together with a genomic clone of rat cytochrome c were used as probes to quantitate the respective RNA transcription rates in isolated nuclei run off transcription assays from stationary cells cultured under normal or 2% oxygen. The transcription rates of lactate dehydrogenase, pyruvate kinase, triosephosphate isomerase and aldolase increased by 2–5 fold during the 72 hr exposure to 2% oxygen. There was a small increase in actin RNA transcription while both cytochrome c and glyceraldehyde-3-phosphate dehydrogenase RNA transcription rates decreased. Since previous studies demonstrated an increase in steady state glyceraldehyde-3-phosphate dehydrogenase RNA during low Oz exposure it is concluded that the level of this RNA is regulated post transcriptionally whereas the other four glycolytic enzyme RNAs are regulated at least partially at the level of transcription by oxygen availability. The relative transcriptional rates of the RNAs in this study are related to their cellular RNA and protein concentrations.
97 citations
TL;DR: Specificity of the phosphorylating enzymes toward the nucleoside analog diphosphates is dependent on the configuration of the analog (l or d) and the presence or absence of 3′-hydroxyl group in the sugar moiety.
96 citations