| + |
PSPH | down-regulates quantity 
chemical modification
|
O-phosphonato-L-serine(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268570 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12213811 |
Human phosphoserine phosphatase (HPSP) regulates the levels of glycine and d-serine, the putative co-agonists for the glycine site of the NMDA receptor in the brain. |Phosphoserine phosphatase (PSP)1 is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous l-serine|he enzymatic reaction of PSP is Mg2+-dependent and results in the dephosphorylation of phospho-l-serine with the formation of a phosphoenzyme intermediate, which is subsequently autodephosphorylated. The resulting product, l-serine, is not only a precursor for the biosynthesis of glycine but also an uncompetitive inhibitor for the enzymatic reaction of PSP |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
O-phosphonato-L-serine(2-) | up-regulates quantity 
precursor of
|
L-serine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268569 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12213811 |
Human phosphoserine phosphatase (HPSP) regulates the levels of glycine and d-serine, the putative co-agonists for the glycine site of the NMDA receptor in the brain. |Phosphoserine phosphatase (PSP)1 is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous l-serine|he enzymatic reaction of PSP is Mg2+-dependent and results in the dephosphorylation of phospho-l-serine with the formation of a phosphoenzyme intermediate, which is subsequently autodephosphorylated. The resulting product, l-serine, is not only a precursor for the biosynthesis of glycine but also an uncompetitive inhibitor for the enzymatic reaction of PSP |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
3-phosphonatooxypyruvate(3-) | up-regulates quantity
precursor of
|
O-phosphonato-L-serine(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268563 |
|
|
Arabidopsis thaliana |
|
| pmid |
sentence |
| 30034403 |
Phosphoserine aminotransferase (PSAT) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. |
|
| Publications: |
1 |
Organism: |
Arabidopsis Thaliana |
| + |
PSAT1 | up-regulates activity
chemical modification
|
O-phosphonato-L-serine(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268560 |
|
|
Arabidopsis thaliana |
|
| pmid |
sentence |
| 30034403 |
Phosphoserine aminotransferase (PSAT) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. |
|
| Publications: |
1 |
Organism: |
Arabidopsis Thaliana |
| + |
O-phosphonato-L-serine(2-) | up-regulates quantity
precursor of
|
3-phosphonatooxypyruvate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268564 |
|
|
Arabidopsis thaliana |
|
| pmid |
sentence |
| 30034403 |
Phosphoserine aminotransferase (PSAT) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. |
|
| Publications: |
1 |
Organism: |
Arabidopsis Thaliana |
3.0
O-phosphonato-L-serine(2-)