PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Phosphoenolpyruvate 54-73 pyruvate kinase M1/2 Homo sapiens 0-18 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Phosphoenolpyruvate 54-73 pyruvate kinase M1/2 Homo sapiens 20-24 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Phosphoenolpyruvate 75-78 pyruvate kinase M1/2 Homo sapiens 0-18 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Phosphoenolpyruvate 75-78 pyruvate kinase M1/2 Homo sapiens 20-24 33901643-2 2021 The activation of PKM2 towards tetramer formation may increase affinity towards phosphoenolpyruvate (PEP) and avoidance of the Warburg effect. Phosphoenolpyruvate 80-99 pyruvate kinase M1/2 Homo sapiens 18-22 35610475-2 2022 Pyruvate kinase M1/2 (PKM) is an enzyme that catalyzes the last step in glycolysis, which converts phosphoenolpyruvate to pyruvate. Phosphoenolpyruvate 99-118 pyruvate kinase M1/2 Homo sapiens 0-20 35610475-2 2022 Pyruvate kinase M1/2 (PKM) is an enzyme that catalyzes the last step in glycolysis, which converts phosphoenolpyruvate to pyruvate. Phosphoenolpyruvate 99-118 pyruvate kinase M1/2 Homo sapiens 22-25 35048565-2 2022 Pyruvate kinase M2 isoform (PKM2) catalyzes the conversion of phosphoenolpyruvate to pyruvate and regulates the last rate-limiting step of glycolysis. Phosphoenolpyruvate 62-81 pyruvate kinase M1/2 Homo sapiens 0-26 35048565-2 2022 Pyruvate kinase M2 isoform (PKM2) catalyzes the conversion of phosphoenolpyruvate to pyruvate and regulates the last rate-limiting step of glycolysis. Phosphoenolpyruvate 62-81 pyruvate kinase M1/2 Homo sapiens 28-32 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Phosphoenolpyruvate 186-205 pyruvate kinase M1/2 Homo sapiens 144-162 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Phosphoenolpyruvate 186-205 pyruvate kinase M1/2 Homo sapiens 164-168 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Phosphoenolpyruvate 207-210 pyruvate kinase M1/2 Homo sapiens 144-162 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Phosphoenolpyruvate 207-210 pyruvate kinase M1/2 Homo sapiens 164-168 33901643-2 2021 The activation of PKM2 towards tetramer formation may increase affinity towards phosphoenolpyruvate (PEP) and avoidance of the Warburg effect. Phosphoenolpyruvate 101-104 pyruvate kinase M1/2 Homo sapiens 18-22 32208360-4 2020 Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis which catalyzes phosphoenolpyruvic acid transforming into pyruvate. Phosphoenolpyruvate 86-109 pyruvate kinase M1/2 Homo sapiens 0-18 33473116-3 2021 Herein we found that SUMOylation of the M2 isoform of pyruvate kinase (PKM2), a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate, is prevalent in a variety of leukemic cell lines as well as primary samples from patients with leukemia through multiple-reaction monitoring based targeted mass spectrometry analysis. Phosphoenolpyruvate 148-167 pyruvate kinase M1/2 Homo sapiens 71-75 33526685-5 2021 This was confirmed by using 13C-labeled flux measurements and immunoblotting, revealing that the key regulatory step of phosphoenolpyruvate to pyruvate was inhibited via down-regulation of the tetrameric pyruvate kinase M2 (PKM2). Phosphoenolpyruvate 120-139 pyruvate kinase M1/2 Homo sapiens 204-222 33526685-5 2021 This was confirmed by using 13C-labeled flux measurements and immunoblotting, revealing that the key regulatory step of phosphoenolpyruvate to pyruvate was inhibited via down-regulation of the tetrameric pyruvate kinase M2 (PKM2). Phosphoenolpyruvate 120-139 pyruvate kinase M1/2 Homo sapiens 224-228 32208360-4 2020 Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis which catalyzes phosphoenolpyruvic acid transforming into pyruvate. Phosphoenolpyruvate 86-109 pyruvate kinase M1/2 Homo sapiens 20-24 29182273-1 2017 Pyruvate kinase muscle isoform 2 (PKM2) catalyzes the terminal step in glycolysis, transferring a phosphoryl group from phosphoenolpyruvate to ADP, to produce pyruvate and ATP. Phosphoenolpyruvate 120-139 pyruvate kinase M1/2 Homo sapiens 0-32 31880514-2 2019 The conversion of phosphoenolpyruvate (PEP) to pyruvate can be down regulated by the re-expression of the embryonic isoform 2 of pyruvate kinase (PKM2). Phosphoenolpyruvate 18-37 pyruvate kinase M1/2 Homo sapiens 146-150 31880514-2 2019 The conversion of phosphoenolpyruvate (PEP) to pyruvate can be down regulated by the re-expression of the embryonic isoform 2 of pyruvate kinase (PKM2). Phosphoenolpyruvate 39-42 pyruvate kinase M1/2 Homo sapiens 146-150 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Phosphoenolpyruvate 80-99 pyruvate kinase M1/2 Homo sapiens 0-26 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Phosphoenolpyruvate 80-99 pyruvate kinase M1/2 Homo sapiens 28-32 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Phosphoenolpyruvate 101-104 pyruvate kinase M1/2 Homo sapiens 0-26 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Phosphoenolpyruvate 101-104 pyruvate kinase M1/2 Homo sapiens 28-32 30087897-7 2018 Furthermore, recent studies have shown that PKM2 is also able to act as a protein kinase using phosphoenolpyruvate (PEP) as a substrate to promote tumorigenesis. Phosphoenolpyruvate 95-114 pyruvate kinase M1/2 Homo sapiens 44-48 30087897-7 2018 Furthermore, recent studies have shown that PKM2 is also able to act as a protein kinase using phosphoenolpyruvate (PEP) as a substrate to promote tumorigenesis. Phosphoenolpyruvate 116-119 pyruvate kinase M1/2 Homo sapiens 44-48 29182273-1 2017 Pyruvate kinase muscle isoform 2 (PKM2) catalyzes the terminal step in glycolysis, transferring a phosphoryl group from phosphoenolpyruvate to ADP, to produce pyruvate and ATP. Phosphoenolpyruvate 120-139 pyruvate kinase M1/2 Homo sapiens 34-38 27152240-1 2016 Pyruvate kinase is a key enzyme in the glycolytic pathway that converts phosphoenolpyruvate to pyruvate, and the M2 isoform of pyruvate kinase (PKM2) is associated with cancer. Phosphoenolpyruvate 72-91 pyruvate kinase M1/2 Homo sapiens 144-148 29312595-1 2017 Pyruvate kinase (PK) catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP, a rate-limiting reaction in glycolysis. Phosphoenolpyruvate 49-68 pyruvate kinase M1/2 Homo sapiens 17-19 27810895-1 2016 The pyruvate kinase (PK) is a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate, yielding one molecule of ATP. Phosphoenolpyruvate 98-117 pyruvate kinase M1/2 Homo sapiens 21-23 23576436-1 2013 Pyruvate kinase isoform M2 (PKM2) is an enzyme-catalyzing conversion of phosphoenolpyruvate to pyruvate in the glycolysis pathway. Phosphoenolpyruvate 72-91 pyruvate kinase M1/2 Homo sapiens 0-26 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Phosphoenolpyruvate 43-62 pyruvate kinase M1/2 Homo sapiens 0-26 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Phosphoenolpyruvate 43-62 pyruvate kinase M1/2 Homo sapiens 28-32 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Phosphoenolpyruvate 64-67 pyruvate kinase M1/2 Homo sapiens 0-26 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Phosphoenolpyruvate 64-67 pyruvate kinase M1/2 Homo sapiens 28-32 23576436-1 2013 Pyruvate kinase isoform M2 (PKM2) is an enzyme-catalyzing conversion of phosphoenolpyruvate to pyruvate in the glycolysis pathway. Phosphoenolpyruvate 72-91 pyruvate kinase M1/2 Homo sapiens 28-32 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 82-101 pyruvate kinase M1/2 Homo sapiens 0-26 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 82-101 pyruvate kinase M1/2 Homo sapiens 28-32 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 103-106 pyruvate kinase M1/2 Homo sapiens 0-26 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 103-106 pyruvate kinase M1/2 Homo sapiens 28-32 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 153-156 pyruvate kinase M1/2 Homo sapiens 0-26 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Phosphoenolpyruvate 153-156 pyruvate kinase M1/2 Homo sapiens 28-32 20847263-4 2010 We demonstrate that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells. Phosphoenolpyruvate 20-39 pyruvate kinase M1/2 Homo sapiens 247-251 22262476-6 2011 Cell growth signals further decrease PKM2 activity, and cells with less active PKM2 use another pathway with separate regulatory properties to convert PEP to pyruvate. Phosphoenolpyruvate 151-154 pyruvate kinase M1/2 Homo sapiens 79-83 20847263-4 2010 We demonstrate that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells. Phosphoenolpyruvate 41-44 pyruvate kinase M1/2 Homo sapiens 247-251 18298799-8 2008 PKM2 exists in either an active tetrameric form which has high affinity for its substrate phosphoenolpyruvate (PEP) or a less active dimeric form which has low affinity for its substrate. Phosphoenolpyruvate 90-109 pyruvate kinase M1/2 Homo sapiens 0-4