| + |
TKT | up-regulates quantity 
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267088 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929114 |
Transketolase (TK, EC 2.2.1.1) is the key rate-limiting enzyme of the non-oxidative branch of the pentose phosphate pathway of carbohydrate transformation. TKs (with the exception of the enzymes of mammalian origin) are characterized by broad substrate specificity. Xylulose 5-phosphate (X5P), fructose 6-phosphate (F6P), erythrulose 4-phosphate, and sedoheptulose 7-phosphate are typical donor substrates of TK; ribose 5-phosphate (R5P), glyceraldehyde 3-phosphate (G3P), and erythrose 4-phosphate are typical acceptor substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
GAPDH | down-regulates quantity 
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266495 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11724794 |
GAPDH is commonly known as a key enzyme in glycolysis (GAPDH catalyzes the NAD-mediated oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate), a number of intriguing intracellular roles have been reported including modulation of the cytoskeleton, kinase activity, and the promotion of vesicle fusion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
D-glyceraldehyde 3-phosphate(2-) | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268134 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis, Pentose phosphate pathway |
| + |
D-ribofuranose 5-phosphate(2-) | up-regulates quantity
precursor of
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268142 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929114 |
Transketolase (TK, EC 2.2.1.1) is the key rate-limiting enzyme of the non-oxidative branch of the pentose phosphate pathway of carbohydrate transformation. TKs (with the exception of the enzymes of mammalian origin) are characterized by broad substrate specificity. Xylulose 5-phosphate (X5P), fructose 6-phosphate (F6P), erythrulose 4-phosphate, and sedoheptulose 7-phosphate are typical donor substrates of TK; ribose 5-phosphate (R5P), glyceraldehyde 3-phosphate (G3P), and erythrose 4-phosphate are typical acceptor substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
2-deoxy-D-ribofuranose 5-phosphate(2-) | up-regulates quantity
precursor of
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267096 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25229427 |
Deoxyribose-phosphate aldolase (EC 4.1.2.4), which converts 2-deoxy-d-ribose-5-phosphate into glyceraldehyde-3-phosphate and acetaldehyde, belongs to the core metabolism of living organisms. his study provides the first experimental evidence that DERA, which is mainly expressed in lung, liver and colon, is the human deoxyribose phosphate aldolase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
D-glyceraldehyde 3-phosphate(2-) | up-regulates quantity
precursor of
|
3-phosphonato-D-glyceroyl phosphate(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11724794 |
GAPDH is commonly known as a key enzyme in glycolysis (GAPDH catalyzes the NAD-mediated oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate), a number of intriguing intracellular roles have been reported including modulation of the cytoskeleton, kinase activity, and the promotion of vesicle fusion |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266493 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11724794 |
GAPDH is commonly known as a key enzyme in glycolysis (GAPDH catalyzes the NAD-mediated oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate), a number of intriguing intracellular roles have been reported including modulation of the cytoskeleton, kinase activity, and the promotion of vesicle fusion |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
D-xylulose 5-phosphate(2-) | up-regulates quantity
precursor of
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268141 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24929114 |
Transketolase (TK, EC 2.2.1.1) is the key rate-limiting enzyme of the non-oxidative branch of the pentose phosphate pathway of carbohydrate transformation. TKs (with the exception of the enzymes of mammalian origin) are characterized by broad substrate specificity. Xylulose 5-phosphate (X5P), fructose 6-phosphate (F6P), erythrulose 4-phosphate, and sedoheptulose 7-phosphate are typical donor substrates of TK; ribose 5-phosphate (R5P), glyceraldehyde 3-phosphate (G3P), and erythrose 4-phosphate are typical acceptor substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
beta-D-fructofuranose 1,6-bisphosphate(4-) | up-regulates quantity
precursor of
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266475 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266476 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
D-glyceraldehyde 3-phosphate(2-) | up-regulates quantity
precursor of
|
D-erythrose 4-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268132 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
GAPDHS | down-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266498 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11724794 |
GAPDH is commonly known as a key enzyme in glycolysis (GAPDH catalyzes the NAD-mediated oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate), a number of intriguing intracellular roles have been reported including modulation of the cytoskeleton, kinase activity, and the promotion of vesicle fusion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
ALDOA | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266479 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
TPI1 | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266492 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Triosephosphate isomerase (TPI) is the glycolytic enzyme with the highest activity in vitro. TPI catalyzes the interconversion of glyceraldehyde-3-phosphate and DHAP (Figure 1). It consists of a dimer with 2 identical subunits of 248 amino acids (27 kDa). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
Aldolase | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266482 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
ALDOC | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266481 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
ALDOB | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266480 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Aldolase catalyzes the reversible conversion of FBP to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (DHAP; Figure 1). Aldolase is a tetramer of identical subunits of 40 kDa each, and 3 distinct isoenzymes have been identified: aldolase A, B, and C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
glycerone phosphate(2-) | up-regulates quantity
precursor of
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268136 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Triosephosphate isomerase (TPI) is the glycolytic enzyme with the highest activity in vitro. TPI catalyzes the interconversion of glyceraldehyde-3-phosphate and DHAP (Figure 1). It consists of a dimer with 2 identical subunits of 248 amino acids (27 kDa). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
TALDO1 | down-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
DERA | up-regulates quantity
chemical modification
|
D-glyceraldehyde 3-phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267098 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25229427 |
Deoxyribose-phosphate aldolase (EC 4.1.2.4), which converts 2-deoxy-d-ribose-5-phosphate into glyceraldehyde-3-phosphate and acetaldehyde, belongs to the core metabolism of living organisms. his study provides the first experimental evidence that DERA, which is mainly expressed in lung, liver and colon, is the human deoxyribose phosphate aldolase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
3.0
D-glyceraldehyde 3-phosphate(2-)