| + |
phenylalanine | up-regulates quantity 
precursor of
|
tyrosine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264172 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK536726 |
L-phenylalanine is converted into L-tyrosine in the liver, by the enzyme phenylalanine hydroxylase (PH) in the presence of oxygen, iron, and tetrahydrobiopterin as cofactors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Catecholamine metabolism |
| + |
Phenylalanyl-tRNA synthetase | down-regulates quantity 
chemical modification
|
phenylalanine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270439 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20223217 |
Here we report crystal structure of hcPheRS complexed with phenylalanine at 3.3 Å resolution. An essential feature of hcPheRS is a novel fold formed by the N-terminal part of the α subunit, whose functional role in tRNAPhe binding and complex formation was studied by truncation mutagenesis. Phenylalanine activation and formation of Phe-tRNAPhe catalyzed by modified hcPheRS have been compared with those of the wild-type enzyme. HcPheRS is a heterotetramer built of two αβ heterodimers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
phenylalanine | up-regulates quantity
|
AminoAcids |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264758 |
|
|
|
|
| pmid |
sentence |
| 29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
| Publications: |
1 |
| + |
PAH | down-regulates quantity
chemical modification
|
phenylalanine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263988 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK536726 |
L-phenylalanine is converted into L-tyrosine in the liver, by the enzyme phenylalanine hydroxylase (PH) in the presence of oxygen, iron, and tetrahydrobiopterin as cofactors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Catecholamine metabolism |
| + |
phenylalanine | up-regulates quantity
precursor of
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270444 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20223217 |
Here we report crystal structure of hcPheRS complexed with phenylalanine at 3.3 Å resolution. An essential feature of hcPheRS is a novel fold formed by the N-terminal part of the α subunit, whose functional role in tRNAPhe binding and complex formation was studied by truncation mutagenesis. Phenylalanine activation and formation of Phe-tRNAPhe catalyzed by modified hcPheRS have been compared with those of the wild-type enzyme. HcPheRS is a heterotetramer built of two αβ heterodimers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
phenylalanine | down-regulates activity
chemical inhibition
|
GCHFR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252205 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11361142 |
The enzyme activity of GTP cyclohydrolase I is controlled by a regulatory protein for this enzyme, GFRP, which is a pentamer of identical subunits. GFRP mediates feedback inhibition of GTP cyclohydrolase I activity by BH4, and the inhibition by BH4 is reversed by phenylalanine |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
phenylalanine