| + |
ATIC | up-regulates quantity 
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267329 |
|
|
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 |
| + |
AMPD1 | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269773 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1631143 |
AMP deaminase (AMPD; EC 3.5.4.6) is encoded by a multigene family in mammals. The AMPD1 gene is expressed at high levels in skeletal muscle, where this enzyme is thought to play an important role in energy metabolism. AMP deaminase (AMPD; EC 3.5.4.6), an enzyme that catalyzes deamination of AMP to IMP, and the purine nucleotide cycle, of which AMPD is one component, play a central role in purine nucleotide interconversion in eukaryotic cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280482 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
IMPDH1 | down-regulates quantity 
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19480389 |
IMPDH controls the gateway to guanine nucleotides, making it an “enzyme of consequence” for virtually every organism. The IMPDH-catalyzed conversion of IMP to XMP is the first committed and rate-limiting step in guanine nucleotide biosynthesis. XMP is subsequently converted to GMP by the action of GMP synthetase (GMPS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
HPRT1 | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10338013 |
Hypoxanthine phosphoribosyltransferase @HGPRTase; EC 2.4.2.8; hypoxanthine pyrophosphate phosphoribosyltransferase# is a purine salvage enzyme that catalyzes the reversible transfer of the 5-phosphoribosyl group between a-d-5-phosphoribosyl-1- pyrophosphate ~PRPP! and a purine base ~hypoxanthine or guanine! to form a purine nucleotide @inosine monophosphate ~IMP! or guanosine monophosphate ~GMP!#. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
hypoxanthine | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10338013 |
Hypoxanthine phosphoribosyltransferase @HGPRTase; EC 2.4.2.8; hypoxanthine pyrophosphate phosphoribosyltransferase# is a purine salvage enzyme that catalyzes the reversible transfer of the 5-phosphoribosyl group between a-d-5-phosphoribosyl-1- pyrophosphate ~PRPP! and a purine base ~hypoxanthine or guanine! to form a purine nucleotide @inosine monophosphate ~IMP! or guanosine monophosphate ~GMP!#. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
5-phospho-α-D-ribose 1-diphosphate | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280479 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10338013 |
Hypoxanthine phosphoribosyltransferase @HGPRTase; EC 2.4.2.8; hypoxanthine pyrophosphate phosphoribosyltransferase# is a purine salvage enzyme that catalyzes the reversible transfer of the 5-phosphoribosyl group between a-d-5-phosphoribosyl-1- pyrophosphate ~PRPP! and a purine base ~hypoxanthine or guanine! to form a purine nucleotide @inosine monophosphate ~IMP! or guanosine monophosphate ~GMP!#. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
AMP | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280484 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280489 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280494 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
AMPD2 | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280487 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPD3 | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280492 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPDA | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280498 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29884623 |
We show that Arabidopsis thaliana and human cells require an N6-mAMP deaminase (ADAL, renamed MAPDA) to catabolize N6-mAMP to inosine monophosphate in vivo by hydrolytically removing the aminomethyl group. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
adenosine 5'-monophosphate | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269774 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1631143 |
AMP deaminase (AMPD; EC 3.5.4.6) is encoded by a multigene family in mammals. The AMPD1 gene is expressed at high levels in skeletal muscle, where this enzyme is thought to play an important role in energy metabolism. AMP deaminase (AMPD; EC 3.5.4.6), an enzyme that catalyzes deamination of AMP to IMP, and the purine nucleotide cycle, of which AMPD is one component, play a central role in purine nucleotide interconversion in eukaryotic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
IMPDH2 | down-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267334 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19480389 |
IMPDH controls the gateway to guanine nucleotides, making it an “enzyme of consequence” for virtually every organism. The IMPDH-catalyzed conversion of IMP to XMP is the first committed and rate-limiting step in guanine nucleotide biosynthesis. XMP is subsequently converted to GMP by the action of GMP synthetase (GMPS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
IMP | up-regulates quantity
precursor of
|
5'-xanthylic acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19480389 |
IMPDH controls the gateway to guanine nucleotides, making it an “enzyme of consequence” for virtually every organism. The IMPDH-catalyzed conversion of IMP to XMP is the first committed and rate-limiting step in guanine nucleotide biosynthesis. XMP is subsequently converted to GMP by the action of GMP synthetase (GMPS). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267330 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19480389 |
IMPDH controls the gateway to guanine nucleotides, making it an “enzyme of consequence” for virtually every organism. Humans and other mammals have two IMPDH genes, encoding hIMPDH1 and hIMPDH2. The IMPDH-catalyzed conversion of IMP to XMP is the first committed and rate-limiting step in guanine nucleotide biosynthesis. XMP is subsequently converted to GMP by the action of GMP synthetase (GMPS). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide(2-) | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267328 |
|
|
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 |
| + |
ADSS1 | down-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267344 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
guanosine 5'-monophosphate(2-) | up-regulates quantity
precursor of
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280515 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33369428 |
The human GMPR enzyme maintains the intracellular balance between the adenine and guanine nucleotide pools. The chemical reaction of this enzyme proceeds by deamination and hydride transfer steps. In deamination, the thiol group of Cys186 reacts on C2 of 5GP to form an intermediate E-XMP. In the second step, nicotinamide moves adjacent to C2 of E-XMP to allow hydride ion transfer, resulting in the production of inosine-5′-monophosphate (IMP) (Figure S4). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IMP | up-regulates quantity
precursor of
|
GDP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268130 |
|
|
|
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
| Pathways: | Nucleotide Biosynthesis |
| + |
IMP | up-regulates 
|
Nucleotide_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280508 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19480389 |
IMPDH controls the gateway to guanine nucleotides, making it an “enzyme of consequence” for virtually every organism. IMP is the product of de novo purine nucleotide biosynthesis and the precursor to both adenine and guanine nucleotides |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GMPR | up-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280512 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33369428 |
The human GMPR enzyme maintains the intracellular balance between the adenine and guanine nucleotide pools. The chemical reaction of this enzyme proceeds by deamination and hydride transfer steps. In deamination, the thiol group of Cys186 reacts on C2 of 5GP to form an intermediate E-XMP. In the second step, nicotinamide moves adjacent to C2 of E-XMP to allow hydride ion transfer, resulting in the production of inosine-5′-monophosphate (IMP) (Figure S4). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADSS2 | down-regulates quantity
chemical modification
|
IMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267343 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
4.0
IMP