+ |
GART | up-regulates quantity
chemical modification
|
N(1)-(5-phospho-beta-D-ribosyl)glycinamide(1-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267300 |
|
|
Homo sapiens |
|
pmid |
sentence |
34283828 |
In humans, GART [phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) / phosphoribosylglycinamide synthetase (EC 6.3.4.13) / phosphoribosylaminoimidazole synthetase (EC 6.3.3.1)] is a trifunctional protein which catalyzes the second, third, and fifth reactions of the ten step de novo purine synthesis (DNPS) pathway. The second step of DNPS is conversion of phosphoribosylamine (5-PRA) to glycineamide ribonucleotide (GAR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
GART | down-regulates quantity
chemical modification
|
glycine |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267299 |
|
|
Homo sapiens |
|
pmid |
sentence |
34283828 |
In humans, GART [phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) / phosphoribosylglycinamide synthetase (EC 6.3.4.13) / phosphoribosylaminoimidazole synthetase (EC 6.3.3.1)] is a trifunctional protein which catalyzes the second, third, and fifth reactions of the ten step de novo purine synthesis (DNPS) pathway. The second step of DNPS is conversion of phosphoribosylamine (5-PRA) to glycineamide ribonucleotide (GAR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
GART | down-regulates quantity
chemical modification
|
5-phospho-beta-D-ribosylaminium(1-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267298 |
|
|
Homo sapiens |
|
pmid |
sentence |
34283828 |
In humans, GART [phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) / phosphoribosylglycinamide synthetase (EC 6.3.4.13) / phosphoribosylaminoimidazole synthetase (EC 6.3.3.1)] is a trifunctional protein which catalyzes the second, third, and fifth reactions of the ten step de novo purine synthesis (DNPS) pathway. The second step of DNPS is conversion of phosphoribosylamine (5-PRA) to glycineamide ribonucleotide (GAR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
GART | down-regulates quantity
chemical modification
|
2-formamido-N(1)-(5-O-phosphonato-beta-D-ribosyl)acetamidine |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267314 |
|
|
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 |
+ |
GART | up-regulates quantity
chemical modification
|
5-amino-1-(5-phosphonato-beta-D-ribosyl)imidazol-3-ium |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267315 |
|
|
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 |
+ |
pemetrexed disodium | down-regulates activity
chemical inhibition
|
GART |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259291 |
|
|
Homo sapiens |
Non-small Cell Lung Cancer Cell |
pmid |
sentence |
14596699 |
Thymidylate synthase, the primary target of pemetrexed,9 is a fo-late-dependent enzyme that catalyzes the transformation of deoxyuri-dine monophosphate to deoxythymidine monophosphate. Inhibi-tion of TS results in decreased levels of thymidine, which is necessary for DNA synthesis. In addition to TS, pemetrexed inhibits DHFR, aminoimidazole carboxamide ribonucleotide formyltransferase (AICARFT), and glycinamide ribonucleotide formyltransferase (GARFT). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GART | up-regulates quantity
chemical modification
|
N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267305 |
|
|
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 |
+ |
pemetrexed | down-regulates
chemical inhibition
|
GART |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-205883 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GART | down-regulates quantity
chemical modification
|
N(1)-(5-phospho-beta-D-ribosyl)glycinamide(1-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268101 |
|
|
Homo sapiens |
|
pmid |
sentence |
34283828 |
In humans, GART [phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) / phosphoribosylglycinamide synthetase (EC 6.3.4.13) / phosphoribosylaminoimidazole synthetase (EC 6.3.3.1)] is a trifunctional protein which catalyzes the second, third, and fifth reactions of the ten step de novo purine synthesis (DNPS) pathway. The second step of DNPS is conversion of phosphoribosylamine (5-PRA) to glycineamide ribonucleotide (GAR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
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 |
+ |
GART | down-regulates quantity
chemical modification
|
10-formyltetrahydrofolate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267303 |
|
|
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 |