| + |
10-formyltetrahydrofolate(2-) | up-regulates quantity 
precursor of
|
formate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268248 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18767138 |
Methylenetetrahydrofolate dehydrogenase)methenyltetrahydrofolate cyclohydrolase)formyltetrahydrofolate synthetase (MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate (THF) derivatives for nucleotide synthesis.|The Arg653Gln substitution is located in the synthetase domain, which catalyzes the magnesium adenosine triphosphate (MgATP)-dependent production of formylTHF from THF and formate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
MTHFD1L | up-regulates quantity
chemical modification
|
formate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268254 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16171773 |
A human mitochondrial isozyme of C1-tetrahydrofolate (THF) synthase was previously identified by its similarity to the human cytoplasmic C1-THF synthase. All C1-THF synthases characterized to date, from yeast to human, are trifunctional, containing the activities of 5,10-methylene-THF dehydrogenase, 5,10-methenyl-THF cyclohydrolase, and 10-formyl-THF synthetase. Here we report on the enzymatic characterization of the recombinant human mitochondrial isozyme. Enzyme assays of purified human mitochondrial C1-THF synthase protein revealed only the presence of 10-formyl-THF synthetase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTHFD1 | up-regulates quantity
chemical modification
|
formate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268251 |
|
|
in vitro |
|
| pmid |
sentence |
| 18767138 |
Methylenetetrahydrofolate dehydrogenase)methenyltetrahydrofolate cyclohydrolase)formyltetrahydrofolate synthetase (MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate (THF) derivatives for nucleotide synthesis.|The Arg653Gln substitution is located in the synthetase domain, which catalyzes the magnesium adenosine triphosphate (MgATP)-dependent production of formylTHF from THF and formate |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | One-carbon Metabolism |
3.0
formate