| + |
L-asparagine zwitterion | up-regulates quantity 
precursor of
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24657844 |
Recently, we structurally and biochemically characterized the enzyme human L-asparaginase 3 (hASNase3), which possesses L-asparaginase activity and belongs to the N-terminal nucleophile superfamily of enzymes. l-Asparaginases (EC 3.5.1.1; l-asparagine amidohydrolase; l-ASNase2) are enzymes that primarily catalyze the conversion of l-asparagine (l-Asn) to l-aspartic acid (l-Asp) and ammonia, although some of them are able to also hydrolyze l-glutamine (l-Gln) to l-glutamic acid (l-Glu) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
L-glutamine zwitterion | up-regulates quantity
precursor of
|
L-asparagine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268071 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
ASNS | up-regulates quantity
chemical modification
|
L-asparagine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267533 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
L-asparagine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268069 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
ASPG | down-regulates quantity 
chemical modification
|
L-asparagine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267537 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24657844 |
Recently, we structurally and biochemically characterized the enzyme human L-asparaginase 3 (hASNase3), which possesses L-asparaginase activity and belongs to the N-terminal nucleophile superfamily of enzymes. l-Asparaginases (EC 3.5.1.1; l-asparagine amidohydrolase; l-ASNase2) are enzymes that primarily catalyze the conversion of l-asparagine (l-Asn) to l-aspartic acid (l-Asp) and ammonia, although some of them are able to also hydrolyze l-glutamine (l-Gln) to l-glutamic acid (l-Glu) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
3.0
L-asparagine zwitterion