| + |
pyruvate | up-regulates quantity 
precursor of
|
oxaloacetate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266553 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24363178 |
As an alternative to decarboxylation by PDH, the second major fate of mitochondrial pyruvate is the irreversible, ATP-dependent carboxylation of pyruvate to oxaloacetate by pyruvate carboxylase (PC). Oxaloacetate is a critical intermediate in metabolism, linking carbohydrate, lipid, amino acid, and nucleotide metabolism (Fig. 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis, Glycolysis and Gluconeogenesis |
| + |
LDHA | down-regulates quantity 
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266918 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929216 |
Glucose and alanine produce pyruvate which is reduced to lactate by lactate dehydrogenase in the cytoplasm without oxygen consumption. Lactate removal takes place via its oxidation to pyruvate by lactate dehydrogenase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
pyruvate | up-regulates quantity
precursor of
|
(S)-lactate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267655 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929216 |
Glucose and alanine produce pyruvate which is reduced to lactate by lactate dehydrogenase in the cytoplasm without oxygen consumption. Lactate removal takes place via its oxidation to pyruvate by lactate dehydrogenase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266920 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929216 |
Glucose and alanine produce pyruvate which is reduced to lactate by lactate dehydrogenase in the cytoplasm without oxygen consumption. Lactate removal takes place via its oxidation to pyruvate by lactate dehydrogenase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PKM | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
phosphonatoenolpyruvate | up-regulates quantity
precursor of
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266532 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266533 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
L-serine | up-regulates quantity
precursor of
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268269 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12393813 |
High levels of d-serine occur in the brain, challenging the notion that d-amino acids would not be present or play a role in mammals. d-serine levels in the brain are even higher than many l-amino acids, such as asparagine, valine, isoleucine, and tryptophan, among others. d-serine is synthesized by a serine racemase (SR) enzyme, which directly converts l- to d-serine. We now report that SR is a bifunctional enzyme, producing both d-serine and pyruvate in cultured cells and in vitro. Transfection of SR into HEK 293 cells elicits synthesis of d-serine and augmented release of pyruvate to culture media. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| Pathways: | One-carbon Metabolism |
| + |
pyruvate | up-regulates quantity
precursor of
|
acetyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266542 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29059435 |
The mitochondrial pyruvate dehydrogenase complex (PDC) irreversibly decarboxylates pyruvate to acetyl coenzyme A, thereby linking glycolysis to the tricarboxylic acid cycle and defining a critical step in cellular bioenergetics. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis, Glycolysis and Gluconeogenesis |
| + |
LDHB | down-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267656 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929216 |
Glucose and alanine produce pyruvate which is reduced to lactate by lactate dehydrogenase in the cytoplasm without oxygen consumption. Lactate removal takes place via its oxidation to pyruvate by lactate dehydrogenase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
(S)-malate(2-) | up-regulates quantity
precursor of
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33064660 |
Malic enzyme 1 (ME1) is a cytosolic protein that catalyzes the conversion of malate to pyruvate while concomitantly generating NADPH from NADP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis |
| + |
PC | down-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266554 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24363178 |
As an alternative to decarboxylation by PDH, the second major fate of mitochondrial pyruvate is the irreversible, ATP-dependent carboxylation of pyruvate to oxaloacetate by pyruvate carboxylase (PC). Oxaloacetate is a critical intermediate in metabolism, linking carbohydrate, lipid, amino acid, and nucleotide metabolism (Fig. 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
L-cysteine zwitterion | up-regulates quantity
precursor of
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275815 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275820 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
SRR | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268268 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12393813 |
High levels of d-serine occur in the brain, challenging the notion that d-amino acids would not be present or play a role in mammals. d-serine levels in the brain are even higher than many l-amino acids, such as asparagine, valine, isoleucine, and tryptophan, among others. d-serine is synthesized by a serine racemase (SR) enzyme, which directly converts l- to d-serine. We now report that SR is a bifunctional enzyme, producing both d-serine and pyruvate in cultured cells and in vitro. Transfection of SR into HEK 293 cells elicits synthesis of d-serine and augmented release of pyruvate to culture media. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
pyruvate | up-regulates activity 
|
Citric_Acid_Cycle |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267384 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18613815 |
Pyruvate carboxylase (PC) is a biotin-containing enzyme that catalyses the HCO3−- and MgATP-dependent carboxylation of pyruvate to form oxaloacetate. This is a very important anaplerotic reaction, replenishing oxaloacetate withdrawn from the Krebs cycle for various pivotal biochemical pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis, Glycolysis and Gluconeogenesis |
| + |
PK | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266540 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
ME1 | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267723 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33064660 |
Malic enzyme 1 (ME1) is a cytosolic protein that catalyzes the conversion of malate to pyruvate while concomitantly generating NADPH from NADP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
PKLR | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266537 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
pyruvate