| + |
(6S)-5,6,7,8-tetrahydrofolate(2-) | up-regulates quantity 
precursor of
|
(6R)-5,10-methylenetetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268225 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32439610 |
Serine catabolism initiated by serine hydroxymethyltransferase (SHMT) transfers thegamma-carbon amino acid side chain to THF, forming glycine and 5,10-methylene-THF (me-THF) (Fig. 1). The cytosolic (SHMT1) and mitochondrial (SHMT2) isoforms perform the same reactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
N(1)-(5-phospho-beta-D-ribosyl)glycinamide(1-) | up-regulates quantity
precursor of
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268103 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33179964 |
The second enzyme in the DNPB pathway is trifunc tional GART (TGART), whose domains and activities include: glycinamide ribonucleotide synthase (GARS) that catalyzes the ATP-dependent process that uses 5- PRA and Gly to make glycinamide ribonucleotide (GAR); glycinamide ribonucleotide transformylase (GART) that transfers the formyl group of N10-formyltetrahydrofolate to GAR, generating formylglycinamide ribonucleotide (FGAR); and aminoimidazole ribonucleotide synthase (AIRS) that converts formylglycinamidine ribonucleotide (FGAM) to aminoimidazole ribonucleotide (AIR) in an ATP-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
10-formyltetrahydrofolate(2-) | up-regulates quantity
precursor of
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267302 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11381136 |
The third step is catalyzed by the enzyme glycinamide ribonucleotide transformylase (GAR Tfase). The two folate-requiring reactions, glycinamide ribonucleotide transformylase (GAR Tfase) and aminoimidazole ribonucleotide transformylase (AICAR Tfase), have attracted particular attention because some of the most successful anticancer drugs to date have been folate antimetabolites such as methotrexate (3). These two enzymes carry out similar chemistry in catalyzing the transfer of a formyl group from 10-formyltetrahydrofolate to the amino group of the substrates GAR and AICAR to form fGAR and fAICAR. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism, Nucleotide Biosynthesis |
| + |
ATIC | up-regulates quantity
chemical modification
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267326 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33179964 |
The last two steps in the pathway are catalyzed by the bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC). The transformylase domain of the enzyme first catalyzes the conversion of AICAR to formylaminoimida zole-4-carboxamide ribonucleotide (FAICAR) using the N10-formyltetrahydrofolate. Then, the cyclohydrolase domain closes the purine ring to form IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide(2-) | up-regulates quantity
precursor of
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267323 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33179964 |
The last two steps in the pathway are catalyzed by the bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC). The transformylase domain of the enzyme first catalyzes the conversion of AICAR to formylaminoimida zole-4-carboxamide ribonucleotide (FAICAR) using the N10-formyltetrahydrofolate. Then, the cyclohydrolase domain closes the purine ring to form IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
dihydrofolate(2-) | up-regulates quantity
precursor of
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268259 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21876184 |
Human dihydrofolate reductase (DHFR) was previously thought to be the only enzyme capable of the reduction of dihydrofolate to tetrahydrofolate; an essential reaction necessary to ensure a continuous supply of biologically active folate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
DHFR2 | up-regulates quantity
chemical modification
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268261 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21876184 |
Human dihydrofolate reductase (DHFR) was previously thought to be the only enzyme capable of the reduction of dihydrofolate to tetrahydrofolate; an essential reaction necessary to ensure a continuous supply of biologically active folate. |We demonstrate that the DHFRP4, or dihydrofolate reductase-like 1 (DHFRL1), gene is expressed and shares some commonalities with DHFR. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DHFR | up-regulates quantity
chemical modification
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268258 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21876184 |
Human dihydrofolate reductase (DHFR) was previously thought to be the only enzyme capable of the reduction of dihydrofolate to tetrahydrofolate; an essential reaction necessary to ensure a continuous supply of biologically active folate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
GART | up-regulates quantity
chemical modification
|
(6S)-5,6,7,8-tetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267304 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11381136 |
The third step is catalyzed by the enzyme glycinamide ribonucleotide transformylase (GAR Tfase). The two folate-requiring reactions, glycinamide ribonucleotide transformylase (GAR Tfase) and aminoimidazole ribonucleotide transformylase (AICAR Tfase), have attracted particular attention because some of the most successful anticancer drugs to date have been folate antimetabolites such as methotrexate (3). These two enzymes carry out similar chemistry in catalyzing the transfer of a formyl group from 10-formyltetrahydrofolate to the amino group of the substrates GAR and AICAR to form fGAR and fAICAR. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
3.0
(6S)-5,6,7,8-tetrahydrofolate(2-)