| + |
CAD | up-regulates quantity 
chemical modification
|
carbamoyl phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267194 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24332717 |
In animals, the first three reactions of the pathway are catalyzed by CAD, an 240 kDa multifunctional protein that combines glutamine-dependent carbamyl phosphate synthetase (GLNCPSase), aspartate transcarbamylase (ATCase), and dihydroorotase (DHOase) activities |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
hydrogencarbonate | up-regulates quantity
precursor of
|
carbamoyl phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267417 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
CAD | down-regulates quantity 
chemical modification
|
carbamoyl phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
CPS1 | up-regulates quantity
chemical modification
|
carbamoyl phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267192 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15096496 |
CPSase catalyzes the synthesis of carbamoyl phosphate from glutamine, bicarbonate, and two ATP molecules |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
carbamoyl phosphate(2-) | up-regulates quantity
precursor of
|
N-carbamoyl-L-aspartate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267422 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
L-glutamine zwitterion | up-regulates quantity
precursor of
|
carbamoyl phosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267416 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267191 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15096496 |
CPSase catalyzes the synthesis of carbamoyl phosphate from glutamine, bicarbonate, and two ATP molecules |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
3.0
carbamoyl phosphate(2-)