+ |
ENO2 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266525 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
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-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). |
|
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). |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
2-phosphonato-D-glycerate(3-) | up-regulates quantity
precursor of
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266521 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266520 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266523 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266522 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
PK | down-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266539 |
|
|
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 |
+ |
ENO3 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266526 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
PCK2 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266557 |
|
|
Homo sapiens |
|
pmid |
sentence |
24632615 |
Phosphoenolpyruvate carboxykinase (PEPCK, EC 4.1.1.32) is a key enzyme of gluconeogenesis. Two isoforms exist, a cytoplasmic form (PCK1, PEPCK-C) and a mitochondrial isoform (PCK2, PEPCK-M). PEPCK activity is present at significant levels in the liver, but also in the kidney and in brown and white adipose tissue. PEPCK, which converts oxaloacetate (OAA) to PEP, has an important role in glucose formation, but also for the generation of glycerol and serine. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
PKLR | down-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266535 |
|
|
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 |
+ |
PKM | down-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266534 |
|
|
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 |
+ |
Enolase | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266527 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
oxaloacetate(2-) | up-regulates quantity
precursor of
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266555 |
|
|
Homo sapiens |
|
pmid |
sentence |
24632615 |
Phosphoenolpyruvate carboxykinase (PEPCK, EC 4.1.1.32) is a key enzyme of gluconeogenesis. Two isoforms exist, a cytoplasmic form (PCK1, PEPCK-C) and a mitochondrial isoform (PCK2, PEPCK-M). PEPCK activity is present at significant levels in the liver, but also in the kidney and in brown and white adipose tissue. PEPCK, which converts oxaloacetate (OAA) to PEP, has an important role in glucose formation, but also for the generation of glycerol and serine. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266586 |
|
|
Homo sapiens |
|
pmid |
sentence |
30193097 |
 PCK1 regulates an essential rate-limiting step by catalyzing the reversible conversion of oxaloacetate (OAA) into phosphoenolpyruvate (PEP).  |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
PCK1 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266587 |
|
|
Homo sapiens |
|
pmid |
sentence |
30193097 |
 PCK1 regulates an essential rate-limiting step by catalyzing the reversible conversion of oxaloacetate (OAA) into phosphoenolpyruvate (PEP).  |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |
+ |
ENO1 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266524 |
|
|
Homo sapiens |
|
pmid |
sentence |
29767008 |
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glycolysis and Gluconeogenesis |